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Enzyme Nomenclature
Information on EC 3.4.22.45 - helper-component proteinase
for references in articles please use BRENDA:EC3.4.22.45
Word Map on EC 3.4.22.45
- 3.4.22.45
-
mosaic
- tobacco
- viruses
- potato
- potyviruses
- nicotiana
-
polyproteins
- benthamiana
-
potyviral
-
etch
- aphid
-
mottle
- potyviridae
- plum
-
turnip
- zucchini
-
cistron
-
streak
-
ringspot
- papaya
-
cucurbit
-
self-interaction
- nia-pro
- tritimovirus
-
non-persistent
-
pvyntn
- agriculture
-
genome-linked
-
rna-silencing
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.4.22.45
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RECOMMENDED NAME
GeneOntology No.
helper-component proteinase
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
124566-20-7
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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
-
-
genome polyprotein, includes helper component proteinase HC-pro; N strain
SwissProt
engineered to encode six histidines within the gene of the HC–Pro
SwissProt
3 different strains, plum pox virus-D, plum pox virus-M, plum pox virus-Rec
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-
genome polyprotein, includes helper component proteinase HC-pro; N strain
SwissProt
engineered to encode six histidines within the gene of the HC–Pro
SwissProt
polyprotein, sequence ID of mutant HC-ProFINK protein is A1DU46; ZYMV
UniProt
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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
Q9DIC2;
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
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. 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
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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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
?
-
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
?
-
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
?
-
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
?
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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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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SUBUNITS
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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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
B2CZ54;, Q06IX7;
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
Q9DIC2;
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
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ENGINEERING
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
Q9DIC2;
mutations in the 4E binding site of HCpro reducing virulence of PVA
additional information
Q9DIC2;
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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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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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.22.45)
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