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Information on EC 3.4.22.45 - helper-component proteinase and Organism(s) Zucchini yellow mosaic virus and UniProt Accession P18479
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3.4.22.45 helper-component proteinaseSpecify your search results
Word Map
- 3.4.22.45
- viruses
- potato
- nicotiana
- potyviruses
- polyproteins
- benthamiana
-
potyviral
- aphid
- potyviridae
-
mottle
-
etch
- turnip
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cistron
- plum
- zucchini
-
ringspot
- papaya
- nia-pro
-
cucurbit
- tritimovirus
-
non-persistent
- ipomovirus
-
pvyntn
-
genome-linked
-
rna-silencing
-
veinal
-
feathery
- agriculture
The taxonomic range for the selected organisms is: Zucchini yellow mosaic virus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
hc-pro, hcpro, helper component-proteinase, helper component proteinase, hc-pro protein, helper-component proteinase, helper component-protease, helper component protease, hc-pro proteinase, pva hc-pro, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HC-Pro
helper component-proteinase
HC-Pro
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-
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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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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
?
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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
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-
?
additional information
?
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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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?
additional information
?
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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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-
?
additional information
?
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the helper component-proteinase of the Zucchini yellow mosaic virus inhibits the Arabidopsis thaliana Hua Enhancer 1 methyltransferase, HEN1, activity in vitro
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?
additional information
?
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analysis of RNA-binding activity of HC-Pro by EMSA, overview
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?
additional information
?
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analysis of RNA-binding activity of HC-Pro by EMSA, overview
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-
?
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
-
-
?
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
?
-
-
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
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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
additional information
zucchini yellow mosaic virus carried within the stylets of aphids, in vitro association between the potyviral helper component protease HCPro protein and a component of the aphid cuticle of the aphid Myzus persicae identified, protein extracts with two HCPro proteins, differing by the presence of amino acid residues K or E in the KLSC domain used for binding studies, HCPro 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
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zucchini yellow mosaic virus carried within the stylets of aphids, in vitro association between the potyviral helper component protease HCPro protein and a component of the aphid cuticle of the aphid Myzus persicae identified, protein extracts with two HCPro proteins, differing by the presence of amino acid residues K or E in the KLSC domain used for binding studies, HCPro 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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
engineered to encode six histidines within the gene of the HCPro
SwissProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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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
a point mutation in the highly conserved FRNK box produces the HC-ProFINK protein that shows no sRNA binding
physiological function
physiological function
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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
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
-
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
99000
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x * 99000, recombinant MBP-tagged wild-type enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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x * 99000, recombinant MBP-tagged wild-type enzyme, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D506Y
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very mild symptoms of zucchini yellow mosaic virus infection
R180I/E396N
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induces transient leaf mottling, affects symptom severity and viral pathogenicity
R180I/F205L/E396N
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the mutant is completely defective in its capacity to block miRNA regulation
additional information
additional information
a point mutation in the highly conserved FRNK box produces the HC-ProFINK protein that shows no sRNA binding
additional information
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a point mutation in the highly conserved FRNK box produces the HC-ProFINK protein that shows no sRNA binding
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
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HC-Pro protein, wild-type and mutant protein, gel filtration
recombinant MBP-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity purification using amylose magnetic beads
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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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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 wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Pea seed-borne mosaic virus, Peanut stripe virus, pepper mottle virus, Plum pox virus, Potato virus Y strain C, potato virus Y, tobacco vein mottling virus, turnip mosaic virus, zucchini yellow mosaic virus
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Maia, I.G.; Haenni, A.L.; Bernardi, F.
Potyviral HC-Pro: a multifunctional protein
J. Gen. Virol.
77
1335-1341
1996
Potato virus Y strain C, potato virus Y, tobacco etch virus, tobacco vein mottling virus, zucchini yellow mosaic virus
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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)
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)
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
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
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
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
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
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