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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| Veröffentlicht in: | Journal of general virology 2011-09, Vol.92 (Pt 9), p.2222-2226 |
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| creator | Jamous, Rana M Boonrod, Kajohn Fuellgrabe, Marc W Ali-Shtayeh, Mohammed S Krczal, Gabi Wassenegger, Michael |
| description | 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. |
| doi_str_mv | 10.1099/vir.0.031534-0 |
| format | Article |
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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.</description><identifier>ISSN: 1465-2099</identifier><identifier>ISSN: 0022-1317</identifier><identifier>EISSN: 1465-2099</identifier><identifier>DOI: 10.1099/vir.0.031534-0</identifier><identifier>PMID: 21593273</identifier><identifier>CODEN: JGVIAY</identifier><language>eng</language><publisher>Reading: Society for General Microbiology</publisher><subject>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</subject><ispartof>Journal of general virology, 2011-09, Vol.92 (Pt 9), p.2222-2226</ispartof><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-8431b5d7a0532df5cb7bbdca3720532bf856f6358e4c935dc78752783637753a3</citedby><cites>FETCH-LOGICAL-c388t-8431b5d7a0532df5cb7bbdca3720532bf856f6358e4c935dc78752783637753a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3733,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24472663$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21593273$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jamous, Rana M</creatorcontrib><creatorcontrib>Boonrod, Kajohn</creatorcontrib><creatorcontrib>Fuellgrabe, Marc W</creatorcontrib><creatorcontrib>Ali-Shtayeh, Mohammed S</creatorcontrib><creatorcontrib>Krczal, Gabi</creatorcontrib><creatorcontrib>Wassenegger, Michael</creatorcontrib><title>helper component-proteinase of the Zucchini yellow mosaic virus inhibits the Hua Enhancer 1 methyltransferase activity in vitro</title><title>Journal of general virology</title><addtitle>J Gen Virol</addtitle><description>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.</description><subject>amino acids</subject><subject>Arabidopsis Proteins - antagonists & inhibitors</subject><subject>bacterial proteins</subject><subject>Biological and medical sciences</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Host-Pathogen Interactions</subject><subject>methyltransferases</subject><subject>Methyltransferases - antagonists & inhibitors</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>mutants</subject><subject>Mutation, Missense</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>Plant viruses and viroids</subject><subject>Potyvirus - enzymology</subject><subject>Potyvirus - pathogenicity</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping</subject><subject>RNA</subject><subject>Sequence Deletion</subject><subject>Viral Proteins - metabolism</subject><subject>Virology</subject><subject>Zucchini yellow mosaic virus</subject><issn>1465-2099</issn><issn>0022-1317</issn><issn>1465-2099</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkb1vFDEQxS1ERJKDlhLcoFR7-HPtLVGULylSipCGxvJ6bdZo1z5sb9BV_Ovx5S6Eakbj37zRewbgI0ZrjLru66NPa7RGFHPKGvQGnGDW8obUp7f_9cfgNOdfCGHGuHgHjgnmHSWCnoC_o502NkET500MNpRmk2KxPuhsYXSwjBb-WIwZffBwa6cp_oFzzNobWE8vGfow-t6X_ExeLxpehFEHUyUxnG0Zt1NJOmRn005Rm-IffdnWtbpfUnwPjpyesv1wqCvwcHnx_fy6ub27ujn_dtsYKmVpJKO454PQiFMyOG560feD0VSQ3aR3kreupVxaZjrKByOk4ERI2lIhONV0Bc72utXe78XmomafTfWjg41LVlIyRhiVpJLrPWlSzDlZpzbJzzptFUZql7mqxhVS-8xrWYFPB-mln-3wD38JuQJfDoDORk-u5mF8fuUYE6Rtd9znPed0VPpnqszDPUG4RfXnqOw6-gR3Q5Uk</recordid><startdate>20110901</startdate><enddate>20110901</enddate><creator>Jamous, Rana M</creator><creator>Boonrod, Kajohn</creator><creator>Fuellgrabe, Marc W</creator><creator>Ali-Shtayeh, Mohammed S</creator><creator>Krczal, Gabi</creator><creator>Wassenegger, Michael</creator><general>Society for General Microbiology</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20110901</creationdate><title>helper component-proteinase of the Zucchini yellow mosaic virus inhibits the Hua Enhancer 1 methyltransferase activity in vitro</title><author>Jamous, Rana M ; Boonrod, Kajohn ; Fuellgrabe, Marc W ; Ali-Shtayeh, Mohammed S ; Krczal, Gabi ; Wassenegger, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-8431b5d7a0532df5cb7bbdca3720532bf856f6358e4c935dc78752783637753a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>amino acids</topic><topic>Arabidopsis Proteins - antagonists & inhibitors</topic><topic>bacterial proteins</topic><topic>Biological and medical sciences</topic><topic>Cysteine Endopeptidases - metabolism</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Host-Pathogen Interactions</topic><topic>methyltransferases</topic><topic>Methyltransferases - antagonists & inhibitors</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>mutants</topic><topic>Mutation, Missense</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>Plant viruses and viroids</topic><topic>Potyvirus - enzymology</topic><topic>Potyvirus - pathogenicity</topic><topic>Protein Binding</topic><topic>Protein Interaction Mapping</topic><topic>RNA</topic><topic>Sequence Deletion</topic><topic>Viral Proteins - metabolism</topic><topic>Virology</topic><topic>Zucchini yellow mosaic virus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jamous, Rana M</creatorcontrib><creatorcontrib>Boonrod, Kajohn</creatorcontrib><creatorcontrib>Fuellgrabe, Marc W</creatorcontrib><creatorcontrib>Ali-Shtayeh, Mohammed S</creatorcontrib><creatorcontrib>Krczal, Gabi</creatorcontrib><creatorcontrib>Wassenegger, Michael</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of general virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jamous, Rana M</au><au>Boonrod, Kajohn</au><au>Fuellgrabe, Marc W</au><au>Ali-Shtayeh, Mohammed S</au><au>Krczal, Gabi</au><au>Wassenegger, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>helper component-proteinase of the Zucchini yellow mosaic virus inhibits the Hua Enhancer 1 methyltransferase activity in vitro</atitle><jtitle>Journal of general virology</jtitle><addtitle>J Gen Virol</addtitle><date>2011-09-01</date><risdate>2011</risdate><volume>92</volume><issue>Pt 9</issue><spage>2222</spage><epage>2226</epage><pages>2222-2226</pages><issn>1465-2099</issn><issn>0022-1317</issn><eissn>1465-2099</eissn><coden>JGVIAY</coden><abstract>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.</abstract><cop>Reading</cop><pub>Society for General Microbiology</pub><pmid>21593273</pmid><doi>10.1099/vir.0.031534-0</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| 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 |
| title | helper component-proteinase of the Zucchini yellow mosaic virus inhibits the Hua Enhancer 1 methyltransferase activity in vitro |
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