helper component-proteinase of the Zucchini yellow mosaic virus inhibits the Hua Enhancer 1 methyltransferase activity in vitro

The helper component-proteinase (HC-Pro) is a multifunctional protein found among potyviruses. With respect to its silencing suppressor function, small RNA binding appears to be the major activity of HC-Pro. HC-Pro could also exhibit other suppressor activities. HC-Pro may inhibit the Hua Enhancer 1...

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Bibliographic Details
Published in:Journal of general virology 2011-09, Vol.92 (Pt 9), p.2222-2226
Main Authors: Jamous, Rana M, Boonrod, Kajohn, Fuellgrabe, Marc W, Ali-Shtayeh, Mohammed S, Krczal, Gabi, Wassenegger, Michael
Format: Article
Language:English
Subjects:
amino acids
Arabidopsis Proteins - antagonists & inhibitors
bacterial proteins
Biological and medical sciences
Cysteine Endopeptidases - metabolism
Enzyme-Linked Immunosorbent Assay
Fundamental and applied biological sciences. Psychology
Host-Pathogen Interactions
methyltransferases
Methyltransferases - antagonists & inhibitors
Microbiology
Miscellaneous
mutants
Mutation, Missense
Phytopathology. Animal pests. Plant and forest protection
Plant viruses and viroids
Potyvirus - enzymology
Potyvirus - pathogenicity
Protein Binding
Protein Interaction Mapping
RNA
Sequence Deletion
Viral Proteins - metabolism
Virology
Zucchini yellow mosaic virus
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Summary:The helper component-proteinase (HC-Pro) is a multifunctional protein found among potyviruses. With respect to its silencing suppressor function, small RNA binding appears to be the major activity of HC-Pro. HC-Pro could also exhibit other suppressor activities. HC-Pro may inhibit the Hua Enhancer 1 (HEN1) activity. There is indirect evidence showing that either transient or stable expression of HC-Pro in plants results in an increase of non-methylated small RNAs. Here, we demonstrated that recombinant Zucchini yellow mosaic virus (ZYMV) HC-Pro inhibited the methyltransferase activity of HEN1 in vitro. Moreover, we found that the HC-ProFINK mutant, which has lost small RNA-binding activity, inhibited HEN1 activity, while the truncated proteins and total soluble bacterial proteins did not. Using the ELISA-binding assay, we provided evidence that the HC-ProFRNK wild-type and HC-ProFINK both bound to HEN1, with HC-ProFRNK binding stronger than HC-ProFINK. Motif mapping analysis revealed that the amino acids located between positions 139 and 320 of ZYMV HC-Pro were associated with HEN1 interaction.
ISSN:1465-2099
0022-1317
1465-2099
DOI:10.1099/vir.0.031534-0