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Information on EC 3.4.22.45 - helper-component proteinase
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3.4.22.45 helper-component proteinaseSpecify your search results
Word Map
- 3.4.22.45
- viruses
- potato
- potyviruses
- nicotiana
- benthamiana
-
polyproteins
-
potyviral
-
etch
- aphid
-
mottle
- potyviridae
-
cistron
-
turnip
- plum
- zucchini
-
ringspot
- tritimovirus
-
cucurbit
- nia-pro
-
rna-silencing
-
non-persistent
- ipomovirus
-
veinal
-
pvyntn
- quinoa
-
genome-linked
- agriculture
The enzyme appears in viruses and cellular organisms
Synonyms
hc-pro, hcpro, helper component-proteinase, helper component proteinase, hc-pro protein, helper component-protease, helper component protease, hc-pro proteinase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HC-Pro
HC-Pro protein
HcPro
helper component protease
helper component proteinase
helper component-proteinase
helper-component proteinase
potyvirus helper component proteinase
additional information
HC-Pro
-
-
-
-
additional information
Tobacco vein mottling potyvirus
-
the enzyme belongs to the C6 peptidase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolyses a Gly-/-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-/-Gly, in the processing of the potyviral polyprotein
endopeptidase; Known from many potyviruses. The helper component-proteinase of the tobacco etch virus is a multifunctional protein with several known activities: the N-terminal region is required for aphid transmission and efficient genome amplification, the central region is required for long-distance movement in plants, and the C-terminal domain has cysteine endopeptidase activity. Type example of peptidase family C6
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
124566-20-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the autoproteolytic activity releases its own C-terminus
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
potyvirus helper component + H2O
?
-
the enzyme cleaves at the C-terminal Gly-/-Gly bond
-
-
?
potyvirus helper component + H2O
?
Tobacco vein mottling potyvirus
-
the enzyme cleaves at the C-terminal Gly-/-Gly bond
-
-
?
additional information
?
-
-
the enzyme suppresses gene silencing, especially by inhibition of silencing-associated plant smRNA modification at the 2'-hydroxyl of the terminal ribose, and enhancing of 3'-methylation of viral siRNAs, overview
-
-
-
additional information
?
-
-
the enzyme is involved in different steps of the viral cycle, aphid transmission, replication, and virus cell-to-cell and systemic movement and is a suppressor of posttranscriptional gene silencing
-
?
additional information
?
-
-
multifunctional HcPro targets the 20S proteasome and affects its enzymic activities, e.g. in RNA trunover, cell division, signal transduction, and translation, overview
-
-
-
additional information
?
-
-
the enzyme shows RNA silencing suppressor activity in transfected Nicotiana benthamiana using Potato virus X, overview
-
-
-
additional information
?
-
the helper component proteinase of potato virus A interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
the helper component proteinase of potato virus A interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
the helper component proteinase of potato virus Y interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
the helper component proteinase of potato virus Y interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
-
the enzyme is a suppressor of post-transcriptional gene silencing
-
-
-
additional information
?
-
-
the enzyme is essential for viral infection of plants and acts as post-transcriptional gene silencer by interferring with miRNA-controlled developmental pathways
-
-
-
additional information
?
-
-
the cleavage site is highly conserved at P4, P2, P1, and P1' positions
-
-
-
additional information
?
-
Q000U0
the helper component proteinase of tobacco etch virus interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
Q000U0
the helper component proteinase of tobacco etch virus interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
Tobacco vein mottling potyvirus
-
the enzyme is essential for viral infection of plants and acts as post-transcriptional gene silencer by interferring with miRNA-controlled developmental pathways
-
-
-
additional information
?
-
Tobacco vein mottling potyvirus
-
the cleavage site is highly conserved at P4, P2, P1, and P1' positions
-
-
-
additional information
?
-
-
the enzyme is required for wheat streak mosaic virus transmission by the wheat curl mite, Aceria tosichella, and cannot be replaced by the enzyme of Turnip mosaic virus or Agropyron mosaic virus, while the enzymes of divergent strains function in eriophyd mite transmission assays, overview
-
-
-
additional information
?
-
-
zinc-finger like motif His13-X2-Cys16-X29-Cys46-X2-Cys49 in the helper component protease HC-Pro found to be essential for vector transmission
-
-
-
additional information
?
-
-
conserved FRNK Box in the helper component proteinase HC-Pro of zucchini yellow mosaic virus identified as a binding region for small RNAs and as a region associated with virus symptoms
-
-
-
additional information
?
-
-
the helper component-proteinase of the Zucchini yellow mosaic virus inhibits the Arabidopsis thaliana Hua Enhancer 1 methyltransferase, HEN1, activity in vitro
-
-
-
additional information
?
-
analysis of RNA-binding activity of HC-Pro by EMSA, overview
-
-
-
additional information
?
-
-
conserved FRNK Box in the helper component proteinase HC-Pro of zucchini yellow mosaic virus identified as a binding region for small RNAs and as a region associated with virus symptoms
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the autoproteolytic activity releases its own C-terminus
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
additional information
?
-
-
the enzyme suppresses gene silencing, especially by inhibition of silencing-associated plant smRNA modification at the 2'-hydroxyl of the terminal ribose, and enhancing of 3'-methylation of viral siRNAs, overview
-
-
-
additional information
?
-
-
the enzyme is involved in different steps of the viral cycle, aphid transmission, replication, and virus cell-to-cell and systemic movement and is a suppressor of posttranscriptional gene silencing
-
?
additional information
?
-
-
multifunctional HcPro targets the 20S proteasome and affects its enzymic activities, e.g. in RNA trunover, cell division, signal transduction, and translation, overview
-
-
-
additional information
?
-
Q9DIC2
the helper component proteinase of potato virus A interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
Q9DIC2
the helper component proteinase of potato virus A interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
G2ZHC9
the helper component proteinase of potato virus Y interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
G2ZHC9
the helper component proteinase of potato virus Y interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
-
the enzyme is a suppressor of post-transcriptional gene silencing
-
-
-
additional information
?
-
-
the enzyme is essential for viral infection of plants and acts as post-transcriptional gene silencer by interferring with miRNA-controlled developmental pathways
-
-
-
additional information
?
-
Q000U0
the helper component proteinase of tobacco etch virus interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
Q000U0
the helper component proteinase of tobacco etch virus interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
-
additional information
?
-
Tobacco vein mottling potyvirus
-
the enzyme is essential for viral infection of plants and acts as post-transcriptional gene silencer by interferring with miRNA-controlled developmental pathways
-
-
-
additional information
?
-
-
the enzyme is required for wheat streak mosaic virus transmission by the wheat curl mite, Aceria tosichella, and cannot be replaced by the enzyme of Turnip mosaic virus or Agropyron mosaic virus, while the enzymes of divergent strains function in eriophyd mite transmission assays, overview
-
-
-
additional information
?
-
-
conserved FRNK Box in the helper component proteinase HC-Pro of zucchini yellow mosaic virus identified as a binding region for small RNAs and as a region associated with virus symptoms
-
-
-
additional information
?
-
-
the helper component-proteinase of the Zucchini yellow mosaic virus inhibits the Arabidopsis thaliana Hua Enhancer 1 methyltransferase, HEN1, activity in vitro
-
-
-
additional information
?
-
-
conserved FRNK Box in the helper component proteinase HC-Pro of zucchini yellow mosaic virus identified as a binding region for small RNAs and as a region associated with virus symptoms
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic of interactions between recombinant His-tagged enzyme and 20S proteasome
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
involvement of helper component protease HC-Pro in necrotic symptom expression in broad bean Vicia faba indicated, characterization of a spontaneous mutant (MM) that does not induce lethal necrosis on broad bean assigned to helper component protease HC-Pro, mutations T27I and D193Y assigned to putative zinc finger domain and to the N-terminal RNA binding domain, respectively, RNA-silencing suppression activity of helper component protease HC-Pro in Nicotiana benthamiana shown to be weakened by both mutations, T27I and D193Y, respectively
additional information
characterization of functional domains of helper component protease HC-Pro involved in RNA-silencing suppression activity determined, systematic analysis of silencing suppression function of helper component protease HC-Pro using pentapeptide-insertion scanning mutagenesis presented, regions with different classes of silencing-suppression activity defined, functional map with information on structural domains, biological functions and mutations affecting silencing-suppressor function or viral synergism indicated
additional information
interaction studies of the HC-Pro protein of potato virus Y with the 20S proteasome complex from Arabidosis thaliana, interaction in living cells confirmed, N-terminal region (residues 1 to 97), central region (residues 98 to 298) and C-terminal region (residues 299 to 456) assigned, N-terminal region of HC-Pro found to be involved in binding to the 20S proteasome complex, virus transmission process and in the interaction with host proteins
additional information
-
HC-Pro down-regulates the accumulation of 3' secondary siRNA, but not 5' secondary and primary siRNA, HC-PRO regulates the accumulation of different siRNAs
additional information
-
TEV virion binding activity of the recombinant enzyme expressed in Pichia pastoris, overview
additional information
-
amino acid substitutions in the helper component protease HC-Pro evaluated for effects on virus transmission by the wheat curl mite Aceria tosichella, vector transmission shown to be abolished after alanine substitution at cysteine residues 16, 46 and 49, measurement by determination of infectivity rate
additional information
-
infectivity assays described, GUS assay performed to assess ability of mutants of HC-Pro protein establishing primary infection foci on inoculated leaves, mutants generated of helper component protease HC-Pro protein summarized, proteinase assays performed to determine whether substitution mutations of HC-Pro protein that altered pathogenicity phenotype also affect auto-proteolysis, in all attenuated mutants retained auto-proteolytic activity of HC-Pro protein observed, activity reduced or absent among mutants unable to establish infection foci
additional information
-
zucchini yellow mosaic virus carried within the stylets of aphids, in vitro association between the potyviral helper component protease HC–Pro protein and a component of the aphid cuticle of the aphid Myzus persicae identified, protein extracts with two HC–Pro proteins, differing by the presence of amino acid residues K or E in the KLSC domain used for binding studies, HC–Pro protein with KLSC but not with ELSC found to bind proteins of Myzus persicae, role of the HC-Pro protein as a putative aphid cuticular receptor suggested
additional information
-
mutant analysis of the conserved FRNK domain in the helper component proteinase HC-Pro, mutation in the FRNK motif of HC-Pro protein attenuates symptoms after virus infection without reducing initial HC-Pro protein levels, FRNK domain identified as a probable point of contact with siRNA and miRNA duplexes, analyzed by small RNA-specific microarray, mobility shift assays and GFP suppression assay, sequence similarity of FRNK motif in potyviruses compared
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
potyvirus, clover yellow vein virus no. 30, induction of lethal necrosis in the broad bean Vicia faba
-
-
brenda
genome polyprotein, includes helper component proteinase HC-pro; N strain
SwissProt
brenda
engineered to encode six histidines within the gene of the HC–Pro
SwissProt
brenda
3 different strains, plum pox virus-D, plum pox virus-M, plum pox virus-Rec
-
-
brenda
genome polyprotein, includes helper component proteinase HC-pro; N strain
SwissProt
brenda
WSMV-Sidney 81, infectious clone pS81-SA analyzed
-
-
brenda
engineered to encode six histidines within the gene of the HC–Pro
SwissProt
brenda
polyprotein, sequence ID of mutant HC-ProFINK protein is A1DU46; ZYMV
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
virus on leaves of Nicotiana benthamiana
-
brenda
additional information
Q000U0
virus on leaves of Nicotiana benthamiana
brenda
additional information
-
virus on leaves of Nicotiana benthamiana
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
amino acids essential for the proteolytic activity of ZYMV HC-Pro are distinct from those of the tobacco etch virus HC-Pro, although the amino acid sequences in the proteolytic active domain are conserved among potyviruses
malfunction
physiological function
malfunction
point mutations introduced to a 4E binding motif identified in the C-terminal region of HCpro debilitate interactions of HCpro with translation initiation factors and are detrimental to the virulence of PVA in plants
malfunction
a point mutation in the highly conserved FRNK box produces the HC-ProFINK protein that shows no sRNA binding
malfunction
-
accumulation of potato virus A is significantly reduced in the HIP2-silenced leaves of Nicotiana benthamiana
malfunction
-
point mutations introduced to a 4E binding motif identified in the C-terminal region of HCpro debilitate interactions of HCpro with translation initiation factors and are detrimental to the virulence of PVA in plants
-
physiological function
-
besides its RNA silencing suppressor, RSS, activity, HC-Pro also exhibits protease, the multifunctional helper component proteinase of potyviruses contains an autoproteolytic function that, together with the protein 1 and NIa proteinase, EC 3.4.22.44, processes the polyprotein into mature proteins
physiological function
-
with respect to its silencing suppressor function, small RNA binding appears to be the major activity of HC-Pro. HC-Pro also exhibits other suppressor activities. HC-Pro inhibits the Arabidopsis thaliana Hua Enhancer 1, HEN1, activity, for suppression of plant RNA silencing as a mechanism of the pathogen for survival in the host cell, overview. The RNA methyltransferase HEN1 is responsible for the 3'-terminal 2'-O-methylation of sRNAs
physiological function
the helper component proteinase of potato virus A interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger. Roles for HCpro and/or translation factors in the potyvirus infection cycle
physiological function
the helper component proteinase of potato virus Y interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger. Roles for HCpro and/or translation factors in the potyvirus infection cycle
physiological function
Q000U0
the helper component proteinase of tobacco etch virus interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger. Roles for HCpro and/or translation factors in the potyvirus infection cycle
physiological function
HC-Pro is a helper component-proteinase which acts as a multifunctional protein in the potyviral life cycle. Apart from its proteolytic activity, HC-Pro has the capacity to bind duplex small RNAs
physiological function
-
the enzyme enhances the stability of its cognate capsid protein, positively affecting the yield of virions and consequently improving the infectivity of the viral progeny. This capacity of the enzyme is involved in the coordination of mutually exclusive activities of the viral genome by controlling correct assembly of capsid protein in stable virions
physiological function
-
the enzyme interacts with the microtubule-associated protein HIP2 in host cells
physiological function
-
the enzyme interacts with the microtubule-associated protein HIP2 in host cells
physiological function
-
interaction of the microtubule-associated host protein HIP2 with viral helper component proteinase is important in infection with potato virus A
physiological function
-
the helper component proteinase of potato virus A interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger. Roles for HCpro and/or translation factors in the potyvirus infection cycle
-
physiological function
-
the enzyme interacts with the microtubule-associated protein HIP2 in host cells
-
physiological function
-
the helper component proteinase of potato virus Y interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger. Roles for HCpro and/or translation factors in the potyvirus infection cycle
-
physiological function
-
the enzyme interacts with the microtubule-associated protein HIP2 in host cells
-
physiological function
-
the helper component proteinase of tobacco etch virus interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger. Roles for HCpro and/or translation factors in the potyvirus infection cycle
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
POLG_BCMNN
3066
0
350390
Swiss-Prot
POLG_PPVRA
3140
0
355581
Swiss-Prot
POLG_TUMVJ
Turnip mosaic virus (strain Japanese)
3164
0
357737
Swiss-Prot
MVP_ZYMVC
991
0
113426
Swiss-Prot
MVP_ZYMVR
996
0
113760
Swiss-Prot
MVP_ZYMVS
997
0
114071
Swiss-Prot
POL2_BAMMU
894
0
98349
Swiss-Prot
POL2_BAYMJ
Barley yellow mosaic virus (strain Japanese II-1)
890
1
98464
Swiss-Prot
MVP_BCMNN
999
0
114541
Swiss-Prot
MVP_PRSVH
1228
0
140607
Swiss-Prot
MVP_PSBMV
1096
0
124210
Swiss-Prot
MVP_TUMVJ
Turnip mosaic virus (strain Japanese)
1043
0
117285
Swiss-Prot
POLG_PRSVH
3344
0
381046
Swiss-Prot
POLG_PSBMV
3206
0
364276
Swiss-Prot
MVP_LMV0
Lettuce mosaic virus (strain 0 / isolate French)
1152
0
130214
Swiss-Prot
POLG_LMV0
Lettuce mosaic virus (strain 0 / isolate French)
3255
0
367571
Swiss-Prot
POLG_ZYMVC
3080
0
350629
Swiss-Prot
POLG_ZYMVR
3083
0
351161
Swiss-Prot
POLG_ZYMVS
3083
0
351033
Swiss-Prot
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53000
-
2 * 53000, the enzyme is a dimer in solution, the N-terminus is not essential for self-interaction, SDS-PAGE
99000
-
x * 99000, recombinant MBP-tagged wild-type enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
-
nested deletion and domain mapping for enzyme analysis, overview
?
-
x * 99000, recombinant MBP-tagged wild-type enzyme, SDS-PAGE
dimer
-
present as a homodimer. The ability to dimerize may be important for aphid transmission, but less so for the other functions of the protein
dimer
-
2 * 53000, the enzyme is a dimer in solution, the N-terminus is not essential for self-interaction, SDS-PAGE
dimer
-
present as a homodimer. The ability to dimerize may be important for aphid transmission, but less so for the other functions of the protein
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
two-dimensional crystal of the recombinant proteins are successfully grown on Ni2+-chelating lipid monolayxers. Comparison of projection maps of negatively stained crystals reveal that the enzyme is composed of two domains separated by a flexible constriction
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D193Y
-
mutants of helper component protease HC-Pro of clover yellow vein virus, generated by site-directed mutagenesis or by PCR-based primer extension mutagenesis, revertant of D193Y also created, single mutant alone does not induce lethal necrosis
I33
-
mutants of helper component protease HC-Pro of clover yellow vein virus generated by site-directed mutagenesis or by PCR-based primer extension mutagenesis
R51I
-
mutants of helper component protease HC-Pro of clover yellow vein virus generated by site-directed mutagenesis or by PCR-based primer extension mutagenesis
T27I
-
mutants of helper component protease HC-Pro of clover yellow vein virus generated by site-directed mutagenesis or by PCR-based primer extension mutagenesis, revertant of T27I also created, single mutant alone does not induce lethal necrosis but retains ability to induce necrotic symptoms
P310A/T311A
-
the mutations disrupt interaction between the enzyme and capsid protein
D446A
-
mutation does not abolish in vitro interaction between helper-component-proteinase and coat protein
E450A
-
mutation does not abolish in vitro interaction between helper-component-proteinase and coat protein
H429A
-
mutation does not abolish in vitro interaction between helper-component-proteinase and coat protein
K432A
-
mutation does not abolish in vitro interaction between helper-component-proteinase and coat protein
K452A
-
mutation does not abolish in vitro interaction between helper-component-proteinase and coat protein
R455A
-
mutation abolishes in vitro interaction between helper-component-proteinase and coat protein
T310A
-
mutation abolishes in vitro interaction between helper-component-proteinase and coat protein
A387E
-
no RNA silencing suppressor activity, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
C390W
-
no RNA silencing suppressor activity, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
C694S
-
mutant is proteolytically active and capable of cell-to-cell and long-distance movements
D421N
-
no RNA silencing suppressor activity, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
D715E
-
mutant is proteolytically active and capable of cell-to-cell and long-distance movements
E273A
-
no RNA silencing suppressor activity, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
E299A/D300A
-
RNA silencing suppressor activity reduced compared to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
E360A/D361A
-
RNA silencing suppressor activity reduced compared to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows mild etching
E443K
-
RNA silencing suppressor activity increased compared to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
E452D
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
I11L
-
RNA silencing suppressor activity increased compared to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
I442M
-
no RNA silencing suppressor activity, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
K309N
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
K454T
-
RNA silencing suppressor activity increased compared to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
N193Y
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
N194D
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
N200S
-
RNA silencing suppressor activity increased compared to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
P311L
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
Q265H
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
R127G
-
no RNA silencing suppressor activity, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
R165G
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
R240A/K241A/H242A
-
no RNA silencing suppressor activity, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
R247A/K248A
-
no RNA silencing suppressor activity, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
S610T
-
mutant is proteolytically active and capable of cell-to-cell and long-distance movements
V135A
-
no RNA silencing suppressor activity, Nicotiana benthamiana plant inoculated with infectious transcript shows no etching
V192A
-
RNA silencing suppressor activity reduced compared to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows mild etching
V355L
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
V419A
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
Y234H
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
Y344S
-
RNA silencing suppressor activity similar to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows mild etching
Y423H
-
RNA silencing suppressor activity increased compared to wild-type, Nicotiana benthamiana plant inoculated with infectious transcript shows etching
C16A
-
substitution mutants introduced into amino-proximal region of helper component protease HC-Pro, vector transmission abolished
D506Y
-
very mild symptoms of zucchini yellow mosaic virus infection
R180I/E396N
-
induces transient leaf mottling, affects symptom severity and viral pathogenicity
R180I/F205L/E396N
-
the mutant is completely defective in its capacity to block miRNA regulation
additional information
additional information
-
inactivation by point mutation HCL134H, inhibits synergism and RNA silencing activity
additional information
random-insertion scanning mutagenesis, generation of an pentapeptide-insertion scanning mutagenesis library of helper component protease HC-Pro, performed by using the mutation generation system F701 MGS, pentapeptide scanning mutants in pBIN61S-HC-Pro mapped by restriction digestion, insertion position determined by sequencing
additional information
-
random-insertion scanning mutagenesis, generation of an pentapeptide-insertion scanning mutagenesis library of helper component protease HC-Pro, performed by using the mutation generation system F701 MGS, pentapeptide scanning mutants in pBIN61S-HC-Pro mapped by restriction digestion, insertion position determined by sequencing
-
additional information
mutations in the 4E binding site of HCpro reducing virulence of PVA
additional information
certain mutations introduced to the short, variable region of the enzyme increase accumulation of the enzyme and prolong the time which it remains effective in suppression of RNA silencing
additional information
-
mutations in the 4E binding site of HCpro reducing virulence of PVA
-
additional information
three deletion mutants designed for HC-Pro protein of potato virus Y, HC-Pro1 (residues 98 to 456), HC-Pro2 (residues 1 to 298) and HC-Pro3 (residues 1 to 97) used for yeast two-hybrid analysis
additional information
-
mutations of a short variable region affect interactions with a microtubule-associated protein and induce necrotic responses in tobacco leaves
additional information
-
three deletion mutants designed for HC-Pro protein of potato virus Y, HC-Pro1 (residues 98 to 456), HC-Pro2 (residues 1 to 298) and HC-Pro3 (residues 1 to 97) used for yeast two-hybrid analysis
-
additional information
-
mutations of a short variable region affect interactions with a microtubule-associated protein and induce necrotic responses in tobacco leaves
-
additional information
-
mutants used in compensatory evolution experiments: E299A (0.6127 RNA-silencing suppression activity relative to wild type, numeration corresponds to the location in the full polyprotein), E360A/D361A (0.1507 RNA-silencing suppression activity relative to wild type, numeration corresponds to the location in the full polyprotein), V192A (0.7388 RNA-silencing suppression activity relative to wild type, numeration corresponds to the location in the full polyprotein), Y423H (1.1020 RNA-silencing suppression activity relative to wild type, numeration corresponds to the location in the full polyprotein), E443K (1.2631 RNA-silencing suppression activity relative to wild type, numeration corresponds to the location in the full polyprotein), K454T (1.1592 RNA-silencing suppression activity relative to wild type, numeration corresponds to the location in the full polyprotein), mutations fixed during compensatory evolution experiments are also characterized by RNA-silencing suppression activity values
additional information
-
mutations of a short variable region affect interactions with a microtubule-associated protein and induce necrotic responses in tobacco leaves
additional information
-
mutations of a short variable region affect interactions with a microtubule-associated protein and induce necrotic responses in tobacco leaves
-
additional information
-
construction of deletion mutants of the enzyme with 5'-proximal deletions of 12 to 720 nucleotides, mutant infection of wheat analysis, overview
additional information
-
mutant generation within coding region of helper component protease HC-Pro protein, nine synonymous substitutions and 15 of 25 non-synonymous substitutions shown to be without phenotypic effect, four non-synonymous substitutions, including one reverting to wild type, shown to disply attenuated systemic infection, six non-synonymous substitutions and one nonsense substitution shown to display abolished systemic infectivity
additional information
-
deletion of the first 93 residues of the N-terminus of ZYMV HC-Pro. Mutation of the conserved Gly456 residue does not affect the autoproteolytic activity of ZYMV HC-Pro
additional information
-
generation of different N- and C-terminal truncated DELTA HC-Pro constructs, i.e. comprising residues 93-456, 114-456, and 139-456, or 1-322, 1-350, and 1-372, construction of recombinant mutant MBP:HA-HC-ProFRNK, MBP:HAHC-ProFINK, and truncated MBP:HA-HC-ProFRNK. HC-ProFRNK/FINK clearly inhibits Arabidopsis thaliana HEN1 activity in vitro. HC-ProFRNK/FINK, but not the truncated proteins HC-Pro 93-456, and HC-Pro 1-372 displaying decreased in vitro affinity for AtHEN1 binding, inhibits the methyltransferase activity of AtHEN1 in vitro
additional information
a point mutation in the highly conserved FRNK box produces the HC-ProFINK protein that shows no sRNA binding
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from transfected plants and from Pichia pastoris GS115, purification of TEV virion particles
-
recombinant HC-Pro protein, SDS-PAGE
recombinant His-tagged enzyme from LMV in plant leaves by nickel affinity chromatography and gel filtration, recombinant Strep-tagged enzyme by ammonum sulfate fractionation and gel filtration
-
recombinant MBP-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity purification using amylose magnetic beads
-
recombinant N-terminally His6-tagged or MBP-fused wild-type enzyme and MBP-fused mutant HC-ProFINK protein from Escherichia coli strain BL21 (DE3) by affinity chromatography
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
14 isolates of turnip mosaic virus, RNA extraction, reverse transctiption, amplification using RT-PCR, cloned into pGEM-T vector for sequence analysis and phylogenetic analysis. HC-Pro genes comprise 1374 nucleotides encoding a polypeptide of 458 amino acids
-
42 isolates of plum pox virus (different types of strains. plum pox virus-D, plum pox virus-M, plum pox virus-Rec). Single-strand conformation polymorphism analysis and low-stringency single specific primer PCR analysis are performed on the HC-Pro region of the genome for genotyping
-
binary constructs for overexpression of helper component proteinase HC-Pro in Tobacco etch virus generated, overexpression in Nicotina benthamiana via infiltration with Agrobacterium tumefaciens shown, binary vector pBin19-GFP used, pHannibal vector used for GFP-silencing inverted-repeat constructs
-
expressed in Escherichia coli and Nicotiana tabacum; expressed in Escherichia coli and Nicotiana tabacum
expressed in Escherichia coli, transformation into Agrobacterium tumefaciens C58C1 by using the binary plant expression vector pBIN61Sa
expression in immature Glycine max cotyledonary explants, co-transfection and co-culture with Agrobacterium tumefaciens strain KYRT1 transfected with a hygromycin phosphotransferase gene, the enzyme enhances recorvery of somatic embryos of Glycine max, effects on gene expression, overview
-
expression of HCPro with YN fused to the HCpro N terminus in Nicotiana benthamiana, and translation initiation factors eIF(iso)4E (Tiso4Eb and Piso4Eb) and eIF4E (T4Ea and P4Eb) of tobacco (T) and potato (P) with YC fused to the N- or C-terminus. Leaves are infiltrated with pairs of Agrobacterium strains expressing tester proteins tagged with the opposite halves of YFP
expression of HCPro with YN fused to the HCpro N terminus in Nicotiana benthamiana, and translation initiation factors eIF(iso)4E (Tiso4Eb and Piso4Eb) and eIF4E (T4Ea and P4Eb) of tobacco (T) and potato (P) with YC fused to the N- or C-terminus. Leaves are infiltrated with pairs of Agrobacterium strains expressing tester proteins tagged with the opposite halves of YFP. Interactions are negative in the YTHS, an artificial system in which protein interactions are tested in the nucleus
expression of His6-tagged or MBP-fused wild-type enzyme and of MBP-fused mutant HC-ProFINK protein in Escherichia coli strain BL21 (DE3)
expression of recombinant His-tagged or Strep-tagged enzyme in LMV in plant leaves
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
fragment of pS81-SA containing the HC-Pro protein coding region used for generation of substitution mutations, ligation into pGEM5zf+ and transformation into Escherichia coli DH5a, 250 PCR-generated clones screened for mutations by single-strand conformation polymorphism SSCP analysis
-
full-length coding sequence of HC-Pro of potato virus Y fused to the GAL4 DNA-binding domain, cloned into pGBKT7 via BamHI/PstI digestion to form pGBKT7-HC-Pro, different plasmid constructs generated, overview of domains and deletion mutants of HC-Pro given, transformation into Saccharomyces cerevisiae after subcloning into pGBKT7
functional expression of wild-type MBP:HA-HC-Pro:GFP and truncated mutant MBP:HA-HC-Pro:GFP N1, i.e. enzyme tagged with HA, GFP, and maltose-binding protein, in Escherichia coli leads to autoproteolytic cleavage of the green fluorescent protein, GFP
-
HC-Pro is indispensable for Papaya ringspot virus infection in zucchini, N-terminus of HC-Pro is involved in systemic infection of PRSV
-
HC-Pro is involved in virulence on Rsv1-genotype soybean (Rsv1 is a single dominant resistance gene), influence of single-point mutations on virulence analyzed
-
in vitro translation of transcripts in rabbit reticulocyte lysate or wheat germ extract, expression in Escherichia coli as His-tagged protein
-
mutations in HC-Pro for analysing virulence on soybean, HC-Pro complementation of viral protein P3 is essential for virulence on Rsv1-genotype soybean (Rsv1 is a single dominant resistance gene)
-
nucleotide and amino acid sequence determination, coding region of 1152 nucleotides, expression of wild-type and deletion mutants in recombinant Wheat streak mosaic virus in wheat
-
plasmid pTEV7DA with an infectious TEV clone used as source of wild-type virus and template for site-directed mutagenesis. Wild-type and mutants are cloned into pBIN61 vector, electroporation of Agrobacterium tumefaciens for transient expression assays and quantification of suppression activity.
-
recombinant expression using Potato virus X, PVX, in Nicotiana benthamiana, expression induces the pathogenicity of the Potato virus X manifesting a necrosis in plant and plant death
-
small and large scale functional expression in Pichia pastoris strain GS115 of the gene fused into the Saccharomyces cerevisiae alpha-mating factor secretory peptide coding region, plant transfection using the Myus persicae aphid vector
-
subcloned into pALTER vector for generation of substitution mutations by site-directed mutagenesis
-
used in yeast two-hybrid system, expressed in Escherichia coli, expressed in onion tissue (fusion protein)
-
expression of HCPro with YN fused to the HCpro N terminus in Nicotiana benthamiana, and translation initiation factors eIF(iso)4E (Tiso4Eb and Piso4Eb) and eIF4E (T4Ea and P4Eb) of tobacco (T) and potato (P) with YC fused to the N- or C-terminus. Leaves are infiltrated with pairs of Agrobacterium strains expressing tester proteins tagged with the opposite halves of YFP
expression of HCPro with YN fused to the HCpro N terminus in Nicotiana benthamiana, and translation initiation factors eIF(iso)4E (Tiso4Eb and Piso4Eb) and eIF4E (T4Ea and P4Eb) of tobacco (T) and potato (P) with YC fused to the N- or C-terminus. Leaves are infiltrated with pairs of Agrobacterium strains expressing tester proteins tagged with the opposite halves of YFP
Q000U0
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
agriculture
-
involvement of helper component protease HC-Pro in necrotic symptom expression in broad bean Vicia faba indicated, functional importance for domains of helper component protease HC-Pro determined
agriculture
pentapeptide-insertion scanning mutagenesis shown to be a tool for functional characterization of plant virus proteins
agriculture
-
pentapeptide-insertion scanning mutagenesis shown to be a tool for functional characterization of plant virus proteins
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kasschau, K.D.; Carrington, J.C.
Requirement for HC-Pro processing during genome amplification of tobacco etch potyvirus
Virology
209
268-273
1995
tobacco etch virus
brenda
Verchot, J.
Potyvirus helper component proteinase
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
677-679
1998
barley yellow mosaic virus, Johnsongrass mosaic virus, papaya ringspot virus, Peanut stripe virus, Pea seed-borne mosaic virus, pepper mottle virus, Plum pox virus, potato virus Y, Potato virus Y strain C, tobacco vein mottling virus, turnip mosaic virus, zucchini yellow mosaic virus
-
brenda
Urcuqui-Inchima, S.; Walter, J.; Drugeon, G.; German-Retana, S.; Haenni, A.L.; Candresse, T.; Bernardi, F.; Le Gall, O.
Potyvirus helper component-proteinase self-interaction in the yeast two-hybrid system and delineation of the interaction domain involved
Virology
258
95-99
1999
lettuce mosaic virus, potato virus Y
brenda
Urcuqui-Inchima, S.; Maia, I.G.; Drugeon, G.; Haenni, A.L.; Bernardi, F.
Effect of mutations within the cys-rich region of potyvirus helper component-proteinase on self-interaction
J. Gen. Virol.
80
2809-2812
1999
potato virus Y
brenda
Andrejeva, J.; Puurand, U.; Merits, A.; Rabenstein, F.; Jarvekulg, L.; Valkonen, J.P.
Potyvirus helper component-proteinase and coat protein (CP) have coordinated functions in virus-host interactions and the same CP motif affects virus transmission and accumulation
J. Gen. Virol.
80
1133-1139
1999
potato virus A
brenda
Maia, I.G.; Bernardi, F.
Nucleic acid-binding properties of a bacterially expressed potato virus Y helper component-proteinase
J. Gen. Virol.
77
869-877
1996
potato virus Y
brenda
Maia, I.G.; Haenni, A.L.; Bernardi, F.
Potyviral HC-Pro: a multifunctional protein
J. Gen. Virol.
77
1335-1341
1996
potato virus Y, Potato virus Y strain C, tobacco etch virus, tobacco vein mottling virus, zucchini yellow mosaic virus
-
brenda
Atreya, C.D.; Pirone, T.P.
Mutational analysis of the helper component-proteinase gene of a potyvirus: effects of amino acid substitutions, deletions, and gene replacement on virulence and aphid transmissibility
Proc. Natl. Acad. Sci. USA
90
11919-11923
1993
tobacco vein mottling virus
brenda
Atreya, C.D.; Atreya, P.L.; Thornbury, D.W.; Pirone, T.P.
Site-directed mutations in the potyvirus HC-Pro gene affect helper component activity, virus accumulation, and symptom expression in infected tobacco plants
Virology
191
106-111
1992
tobacco vein mottling virus
brenda
Carrington, J.C.; Herndon, K.L.
Characterization of the potyviral HC-pro autoproteolytic cleavage site
Virology
187
308-315
1992
tobacco etch virus
brenda
Plisson, C.; Drucker, M.; Blanc, S.; German-Retana, S.; Le Gall, O.; Thomas, D.; Bron, P.
Structural characterization of HC-Pro, a plant virus multifunctional protein
J. Biol. Chem.
278
23753-23761
2003
lettuce mosaic virus
brenda
Verchot-Lubicz, J.
Potyvirus helper component proteinase
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
2
1262-1264
2004
Tobacco vein mottling potyvirus
-
brenda
Verchot-Lubicz, J.
Potyvirus helper component proteinase
Handbook of Proteolytic Enzymes (Barrett, A. J. ; Rawlings, N. D. ; Woessner, J. F. ; eds. )
2
1262-1264
2004
tobacco etch virus
-
brenda
Ruiz-Ferrer, V.; Goytia, E.; Martinez-Garcia, B.; Lopez-Abella, D.; Lopez-Moya, J.J.
Expression of functionally active helper component protein of Tobacco etch potyvirus in the yeast Pichia pastoris
J. Gen. Virol.
85
241-249
2004
tobacco etch virus
brenda
Ballut, L.; Drucker, M.; Pugniere, M.; Cambon, F.; Blanc, S.; Roquet, F.; Candresse, T.; Schmid, H.P.; Nicolas, P.; Gall, O.L.; Badaoui, S.
HcPro, a multifunctional protein encoded by a plant RNA virus, targets the 20S proteasome and affects its enzymic activities
J. Gen. Virol.
86
2595-2603
2005
lettuce mosaic virus
brenda
Stenger, D.C.; Hein, G.L.; Gildow, F.E.; Horken, K.M.; French, R.
Plant virus HC-Pro is a determinant of eriophyid mite transmission
J. Virol.
79
9054-9061
2005
Wheat streak mosaic virus
brenda
Gonzalez-Jara, P.; Atencio, F.A.; Martinez-Garcia, B.; Barajas, D.; Tenllado, F.; Diaz-Ruiz, J.R.
A single amino acid mutation in the Plum pox virus helper component-proteinase gene abolishes both synergistic and RNA silencing suppression activities
Phytopathology
95
894-901
2005
Plum pox virus
brenda
Lim, H.S.; Ko, T.S.; Lambert, K.N.; Kim, H.G.; Korban, S.S.; Hartman, G.L.; Domier, L.L.
Soybean mosaic virus helper component-protease enhances somatic embryo production and stabilizes transgene expression in soybean
Plant Physiol. Biochem.
43
1014-1021
2005
Soybean mosaic virus
brenda
Ebhardt, H.A.; Thi, E.P.; Wang, M.B.; Unrau, P.J.
Extensive 3 modification of plant small RNAs is modulated by helper component-proteinase expression
Proc. Natl. Acad. Sci. USA
102
13398-13403
2005
Cucumber mosaic virus
brenda
Stenger, D.C.; Hein, G.L.; French, R.
Nested deletion analysis of Wheat streak mosaic virus HC-Pro: mapping of domains affecting polyprotein processing and eriophyid mite transmission
Virology
350
465-474
2006
Wheat streak mosaic virus
brenda
Young, B.A.; Hein, G.L.; French, R.; Stenger, D.C.
Substitution of conserved cysteine residues in wheat streak mosaic virus HC-Pro abolishes virus transmission by the wheat curl mite
Arch. Virol.
152
2107-2111
2007
Wheat streak mosaic virus
brenda
Yambao, M.L.; Yagihashi, H.; Sekiguchi, H.; Sekiguchi, T.; Sasaki, T.; Sato, M.; Atsumi, G.; Tacahashi, Y.; Nakahara, K.S.; Uyeda, I.
Point mutations in helper component protease of clover yellow vein virus are associated with the attenuation of RNA-silencing suppression activity and symptom expression in broad bean
Arch. Virol.
153
105-115
2008
clover yellow vein virus
brenda
Stenger, D.C.; Young, B.A.; French, R.
Random mutagenesis of wheat streak mosaic virus HC-Pro: non-infectious interfering mutations in a gene dispensable for systemic infection of plants
J. Gen. Virol.
87
2741-2747
2006
Wheat streak mosaic virus
brenda
Varrelmann, M.; Maiss, E.; Pilot, R.; Palkovics, L.
Use of pentapeptide-insertion scanning mutagenesis for functional mapping of the plum pox virus helper component proteinase suppressor of gene silencing
J. Gen. Virol.
88
1005-1015
2007
Plum pox virus (P17766), Plum pox virus, Plum pox virus PPV (P17766)
brenda
Dombrovsky, A.; Gollop, N.; Chen, S.; Chejanovsky, N.; Raccah, B.
In vitro association between the helper component-proteinase of zucchini yellow mosaic virus and cuticle proteins of Myzus persicae
J. Gen. Virol.
88
1602-1610
2007
zucchini yellow mosaic virus (P18479), zucchini yellow mosaic virus, zucchini yellow mosaic virus ZYMV (P18479)
brenda
Jin, Y.; Ma, D.; Dong, J.; Jin, J.; Li, D.; Deng, C.; Wang, T.
HC-Pro protein of Potato virus Y can interact with three Arabidopsis 20S proteasome subunits in planta
J. Virol.
81
12881-12888
2007
potato virus Y (P18247), potato virus Y, potato virus Y N (P18247)
brenda
Shiboleth, Y.M.; Haronsky, E.; Leibman, D.; Arazi, T.; Wassenegger, M.; Whitham, S.A.; Gaba, V.; Gal-On, A.
The conserved FRNK box in HC-Pro, a plant viral suppressor of gene silencing, is required for small RNA binding and mediates symptom development
J. Virol.
81
13135-13148
2007
zucchini yellow mosaic virus (P18479), zucchini yellow mosaic virus, zucchini yellow mosaic virus ZYMV (P18479)
brenda
L, M.; Y, H.; Schubert, J.; P, X.
Sequence analysis of CP and HC-Pro genes of Turnip mosaiv virus isolates from china
Acta Virol.
52
59-62
2008
turnip mosaic virus
brenda
Gadiou, S.; Safarova, D.; Navratil, M.
Differentiation of Plum pox virus isolates by single-strand conformation polymorphism and low-stringency single specific primer PCR analysis of HC-Pro genome region
Acta Virol.
53
53-56
2009
Plum pox virus
brenda
Torres-Barcelo, C.; Martin, S.; Daros, J.A.; Elena, S.F.
From hypo- to hypersuppression: effect of amino acid substitutions on the RNA-silencing suppressor activity of the Tobacco etch potyvirus HC-Pro
Genetics
180
1039-1049
2008
tobacco etch virus
brenda
Eggenberger, A.L.; Hajimorad, M.R.; Hill, J.H.
Gain of virulence on Rsv1-genotype soybean by an avirulent Soybean mosaic virus requires concurrent mutations in both P3 and HC-Pro
Mol. Plant Microbe Interact.
21
931-936
2008
Soybean mosaic virus
brenda
Hajimorad, M.R.; Eggenberger, A.L.; Hill, J.H.
Adaptation of Soybean mosaic virus avirulent chimeras containing P3 sequences from virulent strains to Rsv1-genotype soybeans is mediated by mutations in HC-Pro
Mol. Plant Microbe Interact.
21
937-946
2008
Soybean mosaic virus
brenda
Zhang, X.; Du, P.; Lu, L.; Xiao, Q.; Wang, W.; Cao, X.; Ren, B.; Wei, C.; Li, Y.
Contrasting effects of HC-Pro and 2b viral suppressors from Sugarcane mosaic virus and Tomato aspermy cucumovirus on the accumulation of siRNAs
Virology
374
351-360
2008
Sugarcane mosaic virus
brenda
Yap, Y.K.; Duangjit, J.; Panyim, S.
N-terminal of Papaya ringspot virus type-W (PRSV-W) helper component proteinase (HC-Pro) is essential for PRSV systemic infection in zucchini
Virus Genes
38
461-467
2009
papaya ringspot virus, papaya ringspot virus type-W
brenda
Li, W.; Hilf, M.E.; Webb, S.E.; Baker, C.A.; Adkins, S.
Presence of P1b and absence of HC-Pro in Squash vein yellowing virus suggests a general feature of the genus Ipomovirus in the family Potyviridae
Virus Res.
135
213-219
2008
no activity in Squash vein yellowing virus
brenda
Ma, P.; Liu, J.; He, H.; Yang, M.; Li, M.; Zhu, X.; Wang, X.
A viral suppressor P1/HC-Pro increases the GFP gene expression in agrobacterium-mediated transient assay
Appl. Biochem. Biotechnol.
158
243-252
2009
tobacco etch virus
brenda
Torres-Barcelo, C.; Daros, J.A.; Elena, S.F.
HC-Pro hypo- and hypersuppressor mutants: differences in viral siRNA accumulation in vivo and siRNA binding activity in vitro
Arch. Virol.
155
251-254
2010
tobacco etch virus
brenda
Desbiez, C.; Girard, M.; Lecoq, H.
A novel natural mutation in HC-Pro responsible for mild symptomatology of Zucchini yellow mosaic virus (ZYMV, Potyvirus) in cucurbits
Arch. Virol.
155
397-401
2010
zucchini yellow mosaic virus
brenda
Mbanzibwa, D.R.; Tian, Y.; Mukasa, S.B.; Valkonen, J.P.
Cassava brown streak virus (Potyviridae) encodes a putative Maf/HAM1 pyrophosphatase implicated in reduction of mutations and a P1 proteinase that suppresses RNA silencing but contains no HC-Pro
J. Virol.
83
6934-6940
2009
no activity in cassava brown streak virus
brenda
Torres-Barcelo, C.; Daros, J.A.; Elena, S.F.
Compensatory molecular evolution of HC-Pro, an RNA-silencing suppressor from a plant RNA virus
Mol. Biol. Evol.
27
543-551
2010
tobacco etch virus
brenda
Mangrauthia, S.K.; Singh, P.; Praveen, S.
Genomics of helper component proteinase reveals effective strategy for papaya ringspot virus resistance
Mol. Biotechnol.
44
22-29
2010
papaya ringspot virus (B2CZ54), papaya ringspot virus, papaya ringspot virus (Q06IX7)
brenda
Wu, H.W.; Lin, S.S.; Chen, K.C.; Yeh, S.D.; Chua, N.H.
Discriminating mutations of HC-Pro of zucchini yellow mosaic virus with differential effects on small RNA pathways involved in viral pathogenicity and symptom development
Mol. Plant Microbe Interact.
23
17-28
2010
zucchini yellow mosaic virus
brenda
Seo, J.K.; Kang, S.H.; Seo, B.Y.; Jung, J.K.; Kim, K.H.
Mutational analysis of interaction between coat protein and helper component-proteinase of Soybean mosaic virus involved in aphid transmission
Mol. Plant Pathol.
11
265-276
2010
Soybean mosaic virus
brenda
Shen, W.; Yan, P.; Gao, L.; Pan, X.; Wu, J.; Zhou, P.
Helper component-proteinase (HC-Pro) protein of Papaya ringspot virus interacts with papaya calreticulin
Mol. Plant Pathol.
11
335-346
2010
papaya ringspot virus
brenda
Fukuzawa, N.; Itchoda, N.; Ishihara, T.; Goto, K.; Masuta, C.; Matsumura, T.
HC-Pro, a potyvirus RNA silencing suppressor, cancels cycling of Cucumber mosaic virus in Nicotiana benthamiana plants
Virus Genes
40
440-446
2010
potato virus Y
brenda
Boonrod, K.; Fuellgrabe, M.W.; Krczal, G.; Wassenegger, M.
Analysis of the autoproteolytic activity of the recombinant helper component proteinase from zucchini yellow mosaic virus
Biol. Chem.
392
937-945
2011
zucchini yellow mosaic virus
brenda
Jamous, R.M.; Boonrod, K.; Fuellgrabe, M.W.; Ali-Shtayeh, M.S.; Krczal, G.; Wassenegger, M.
The helper component-proteinase of the Zucchini yellow mosaic virus inhibits the Hua Enhancer 1 methyltransferase activity in vitro
J. Gen. Virol.
92
2222-2226
2011
zucchini yellow mosaic virus
brenda
Ala-Poikela, M.; Goytia, E.; Haikonen, T.; Rajamaeki, M.L.; Valkonen, J.P.
Helper component proteinase of the genus Potyvirus is an interaction partner of translation initiation factors eIF(iso)4E and eIF4E and contains a 4E binding motif
J. Virol.
85
6784-6794
2011
potato virus A, potato virus A (Q9DIC2), potato virus A PVA-B11 (Q9DIC2), potato virus Y (G2ZHC9), potato virus Y, potato virus Y PVY-Nevski (G2ZHC9), tobacco etch virus (Q000U0), tobacco etch virus TEV-HCH10 (Q000U0)
brenda
Fuellgrabe, M.W.; Boonrod, K.; Jamous, R.; Moser, M.; Shiboleth, Y.; Krczal, G.; Wassenegger, M.
Expression, purification and functional characterization of recombinant Zucchini yellow mosaic virus HC-Pro
Protein Expr. Purif.
75
40-45
2011
zucchini yellow mosaic virus (A1DU45), zucchini yellow mosaic virus
brenda
Siriwan, W.; Takaya, N.; Roytrakul, S.; Chowpongpang, S.
Study of interaction between Papaya ringspot virus HC-Pro and papaya (Carica papaya) proteins
J. Gen. Plant Pathol.
80
264-271
2014
papaya ringspot virus
brenda
Haikonen, T.; Rajamaeki, M.L.; Valkonen, J.P.
Improved silencing suppression and enhanced heterologous protein expression are achieved using an engineered viral helper component proteinase
J. Virol. Methods
193
687-692
2013
potato virus A, potato virus A (Q9DIC2)
brenda
Valli, A.; Gallo, A.; Calvo, M.; de Jesus Perez, J.; Garcia, J.A.
A novel role of the potyviral helper component proteinase contributes to enhance the yield of viral particles
J. Virol.
88
9808-9818
2014
Plum pox virus
brenda
Haikonen, T.; Rajamaeki, M.L.; Tian, Y.P.; Valkonen, J.P.
Mutation of a short variable region in HCpro protein of potato virus A affects interactions with a microtubule-associated protein and induces necrotic responses in tobacco
Mol. Plant Microbe Interact.
26
721-733
2013
potato virus Y, potato virus Y Nevski, tobacco etch virus, tobacco etch virus HCH10
brenda
Haikonen, T.; Rajamaeki, M.L.; Valkonen, J.P.
Interaction of the microtubule-associated host protein HIP2 with viral helper component proteinase is important in infection with potato virus A
Mol. Plant Microbe Interact.
26
734-744
2013
potato virus A
brenda
Lim, H.; Jang, C.; Nam, J.; Li, M.; Hong, J.; Bae, H.; Ju, H.; Kim, H.; Ford, R.; Domier, L.
Characterization of the in vitro activities of the P1 and helper component proteases of Soybean mosaic virus strain G2 and Tobacco vein mottling virus
Plant Pathol. J.
28
197-201
2012
Soybean mosaic virus, tobacco vein mottling virus
-
brenda
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