Functional regulation of PVBV Nuclear Inclusion protein-a protease activity upon interaction with Viral Protein genome-linked and phosphorylation
Abstract Regulation of NIa-Pro is crucial for polyprotein processing and hence, for successful infection of potyviruses. We have examined two novel mechanisms that could regulate NIa-Pro activity. Firstly, the influence of VPg domain on the proteolytic activity of NIa-Pro was investigated. It was sh...
Gespeichert in:
| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2012-01, Vol.422 (2), p.254-264 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 264 |
|---|---|
| container_issue | 2 |
| container_start_page | 254 |
| container_title | Virology (New York, N.Y.) |
| container_volume | 422 |
| creator | Mathur, C Jimsheena, V.K Banerjee, S Makinen, K Gowda, L.R Savithri, H.S |
| description | Abstract Regulation of NIa-Pro is crucial for polyprotein processing and hence, for successful infection of potyviruses. We have examined two novel mechanisms that could regulate NIa-Pro activity. Firstly, the influence of VPg domain on the proteolytic activity of NIa-Pro was investigated. It was shown that the turnover number of the protease increases when these two domains interact ( cis : two-fold; trans : seven-fold) with each other. Secondly, the protease activity of NIa-Pro could also be modulated by phosphorylation at Ser129. A mutation of this residue either to aspartate (phosphorylation-mimic) or alanine (phosphorylation-deficient) drastically reduces the protease activity. Based on these observations and molecular modeling studies, we propose that interaction with VPg as well as phosphorylation of Ser129 could relay a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro. |
| doi_str_mv | 10.1016/j.virol.2011.10.009 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_osti_scitechconnect_22149253</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>1_s2_0_S0042682211004788</els_id><sourcerecordid>918055005</sourcerecordid><originalsourceid>FETCH-LOGICAL-c518t-4c268d62661ab0ad7b12c6c11fb8e7d15d680539833adcbe234e069c9d012e783</originalsourceid><addsrcrecordid>eNqFUt1uFCEUJkZj1-oTmBgSL7yalZ8ZBi400cZqk0abqHtLGDjbZTsLW5hZs4_hG8t0qhfe9ILAge8nh-8g9JKSJSVUvN0uDz7FfskIpeVmSYh6hBaUKFERXtPHaEFIzSohGTtBz3LeklK3LXmKThgjSikhF-j3-Rjs4GMwPU5wPfZmKnBc46vVxxX-OtoeTMIXwfZjnl72KQ7gQ2Xmk8mATRE4-OGIx30B-DBAMnea-JcfNnjlUxG_mnn4GkLcQdX7cAMOm-DwfhNzWek4ez9HT9amz_Difj9FP88__Tj7Ul1--3xx9uGysg2VQ1VbJqQTTAhqOmJc21FmhaV03UloHW2ckKThSnJunO2A8RqIUFY5Qhm0kp-i17NuzIPX2foB7MbGEMAOmjFaK9bwgnozo0q3tyPkQe98ttD3JkAcs1a0uDSkOD2M5HXNBK8Lks9Im2LOCdZ6n_zOpKOmRE_R6q2-i1ZP0U6XJdrCenWvP3Y7cP84f7MsgHczAMqvHTykqSkIFpxPU08u-gcM3v_HtyUlb01_A0fI2zimMiVZU52ZJvr7NF3TcFE6zZWU_A9XMs0N</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>913442634</pqid></control><display><type>article</type><title>Functional regulation of PVBV Nuclear Inclusion protein-a protease activity upon interaction with Viral Protein genome-linked and phosphorylation</title><source>Elsevier ScienceDirect Journals Complete - AutoHoldings</source><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>Mathur, C ; Jimsheena, V.K ; Banerjee, S ; Makinen, K ; Gowda, L.R ; Savithri, H.S</creator><creatorcontrib>Mathur, C ; Jimsheena, V.K ; Banerjee, S ; Makinen, K ; Gowda, L.R ; Savithri, H.S</creatorcontrib><description>Abstract Regulation of NIa-Pro is crucial for polyprotein processing and hence, for successful infection of potyviruses. We have examined two novel mechanisms that could regulate NIa-Pro activity. Firstly, the influence of VPg domain on the proteolytic activity of NIa-Pro was investigated. It was shown that the turnover number of the protease increases when these two domains interact ( cis : two-fold; trans : seven-fold) with each other. Secondly, the protease activity of NIa-Pro could also be modulated by phosphorylation at Ser129. A mutation of this residue either to aspartate (phosphorylation-mimic) or alanine (phosphorylation-deficient) drastically reduces the protease activity. Based on these observations and molecular modeling studies, we propose that interaction with VPg as well as phosphorylation of Ser129 could relay a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2011.10.009</identifier><identifier>PMID: 22099968</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; ALANINES ; Base Sequence ; Chromatography, Thin Layer ; Circular Dichroism ; CONFORMATIONAL CHANGES ; Endopeptidases - genetics ; Endopeptidases - metabolism ; Gene Expression Regulation, Viral - physiology ; Genome, Viral ; HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY ; HPLC-based protease assay ; Infectious Disease ; Molecular modeling ; Mutation ; Nuclear Inclusion protein-a protease (NIa-Pro) ; Pepper Vein Banding Virus (PVBV) ; PHOSPHORYLATION ; PHOSPHOTRANSFERASES ; Potyviridae ; Potyvirus - metabolism ; RNA, Viral - chemistry ; RNA, Viral - genetics ; RNA, Viral - metabolism ; Spectrometry, Fluorescence ; VEINS ; Viral Protein genome-linked (VPg) ; Viral Proteins - genetics ; Viral Proteins - metabolism ; VIRUSES ; VPg-Pro</subject><ispartof>Virology (New York, N.Y.), 2012-01, Vol.422 (2), p.254-264</ispartof><rights>Elsevier Inc.</rights><rights>2011 Elsevier Inc.</rights><rights>Copyright © 2011 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c518t-4c268d62661ab0ad7b12c6c11fb8e7d15d680539833adcbe234e069c9d012e783</citedby><cites>FETCH-LOGICAL-c518t-4c268d62661ab0ad7b12c6c11fb8e7d15d680539833adcbe234e069c9d012e783</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.virol.2011.10.009$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,778,782,883,3539,27911,27912,45982</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22099968$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/22149253$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Mathur, C</creatorcontrib><creatorcontrib>Jimsheena, V.K</creatorcontrib><creatorcontrib>Banerjee, S</creatorcontrib><creatorcontrib>Makinen, K</creatorcontrib><creatorcontrib>Gowda, L.R</creatorcontrib><creatorcontrib>Savithri, H.S</creatorcontrib><title>Functional regulation of PVBV Nuclear Inclusion protein-a protease activity upon interaction with Viral Protein genome-linked and phosphorylation</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Abstract Regulation of NIa-Pro is crucial for polyprotein processing and hence, for successful infection of potyviruses. We have examined two novel mechanisms that could regulate NIa-Pro activity. Firstly, the influence of VPg domain on the proteolytic activity of NIa-Pro was investigated. It was shown that the turnover number of the protease increases when these two domains interact ( cis : two-fold; trans : seven-fold) with each other. Secondly, the protease activity of NIa-Pro could also be modulated by phosphorylation at Ser129. A mutation of this residue either to aspartate (phosphorylation-mimic) or alanine (phosphorylation-deficient) drastically reduces the protease activity. Based on these observations and molecular modeling studies, we propose that interaction with VPg as well as phosphorylation of Ser129 could relay a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>ALANINES</subject><subject>Base Sequence</subject><subject>Chromatography, Thin Layer</subject><subject>Circular Dichroism</subject><subject>CONFORMATIONAL CHANGES</subject><subject>Endopeptidases - genetics</subject><subject>Endopeptidases - metabolism</subject><subject>Gene Expression Regulation, Viral - physiology</subject><subject>Genome, Viral</subject><subject>HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY</subject><subject>HPLC-based protease assay</subject><subject>Infectious Disease</subject><subject>Molecular modeling</subject><subject>Mutation</subject><subject>Nuclear Inclusion protein-a protease (NIa-Pro)</subject><subject>Pepper Vein Banding Virus (PVBV)</subject><subject>PHOSPHORYLATION</subject><subject>PHOSPHOTRANSFERASES</subject><subject>Potyviridae</subject><subject>Potyvirus - metabolism</subject><subject>RNA, Viral - chemistry</subject><subject>RNA, Viral - genetics</subject><subject>RNA, Viral - metabolism</subject><subject>Spectrometry, Fluorescence</subject><subject>VEINS</subject><subject>Viral Protein genome-linked (VPg)</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><subject>VIRUSES</subject><subject>VPg-Pro</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUt1uFCEUJkZj1-oTmBgSL7yalZ8ZBi400cZqk0abqHtLGDjbZTsLW5hZs4_hG8t0qhfe9ILAge8nh-8g9JKSJSVUvN0uDz7FfskIpeVmSYh6hBaUKFERXtPHaEFIzSohGTtBz3LeklK3LXmKThgjSikhF-j3-Rjs4GMwPU5wPfZmKnBc46vVxxX-OtoeTMIXwfZjnl72KQ7gQ2Xmk8mATRE4-OGIx30B-DBAMnea-JcfNnjlUxG_mnn4GkLcQdX7cAMOm-DwfhNzWek4ez9HT9amz_Difj9FP88__Tj7Ul1--3xx9uGysg2VQ1VbJqQTTAhqOmJc21FmhaV03UloHW2ckKThSnJunO2A8RqIUFY5Qhm0kp-i17NuzIPX2foB7MbGEMAOmjFaK9bwgnozo0q3tyPkQe98ttD3JkAcs1a0uDSkOD2M5HXNBK8Lks9Im2LOCdZ6n_zOpKOmRE_R6q2-i1ZP0U6XJdrCenWvP3Y7cP84f7MsgHczAMqvHTykqSkIFpxPU08u-gcM3v_HtyUlb01_A0fI2zimMiVZU52ZJvr7NF3TcFE6zZWU_A9XMs0N</recordid><startdate>20120120</startdate><enddate>20120120</enddate><creator>Mathur, C</creator><creator>Jimsheena, V.K</creator><creator>Banerjee, S</creator><creator>Makinen, K</creator><creator>Gowda, L.R</creator><creator>Savithri, H.S</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>OTOTI</scope></search><sort><creationdate>20120120</creationdate><title>Functional regulation of PVBV Nuclear Inclusion protein-a protease activity upon interaction with Viral Protein genome-linked and phosphorylation</title><author>Mathur, C ; Jimsheena, V.K ; Banerjee, S ; Makinen, K ; Gowda, L.R ; Savithri, H.S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c518t-4c268d62661ab0ad7b12c6c11fb8e7d15d680539833adcbe234e069c9d012e783</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>ALANINES</topic><topic>Base Sequence</topic><topic>Chromatography, Thin Layer</topic><topic>Circular Dichroism</topic><topic>CONFORMATIONAL CHANGES</topic><topic>Endopeptidases - genetics</topic><topic>Endopeptidases - metabolism</topic><topic>Gene Expression Regulation, Viral - physiology</topic><topic>Genome, Viral</topic><topic>HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY</topic><topic>HPLC-based protease assay</topic><topic>Infectious Disease</topic><topic>Molecular modeling</topic><topic>Mutation</topic><topic>Nuclear Inclusion protein-a protease (NIa-Pro)</topic><topic>Pepper Vein Banding Virus (PVBV)</topic><topic>PHOSPHORYLATION</topic><topic>PHOSPHOTRANSFERASES</topic><topic>Potyviridae</topic><topic>Potyvirus - metabolism</topic><topic>RNA, Viral - chemistry</topic><topic>RNA, Viral - genetics</topic><topic>RNA, Viral - metabolism</topic><topic>Spectrometry, Fluorescence</topic><topic>VEINS</topic><topic>Viral Protein genome-linked (VPg)</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - metabolism</topic><topic>VIRUSES</topic><topic>VPg-Pro</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mathur, C</creatorcontrib><creatorcontrib>Jimsheena, V.K</creatorcontrib><creatorcontrib>Banerjee, S</creatorcontrib><creatorcontrib>Makinen, K</creatorcontrib><creatorcontrib>Gowda, L.R</creatorcontrib><creatorcontrib>Savithri, H.S</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>OSTI.GOV</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mathur, C</au><au>Jimsheena, V.K</au><au>Banerjee, S</au><au>Makinen, K</au><au>Gowda, L.R</au><au>Savithri, H.S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional regulation of PVBV Nuclear Inclusion protein-a protease activity upon interaction with Viral Protein genome-linked and phosphorylation</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2012-01-20</date><risdate>2012</risdate><volume>422</volume><issue>2</issue><spage>254</spage><epage>264</epage><pages>254-264</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Abstract Regulation of NIa-Pro is crucial for polyprotein processing and hence, for successful infection of potyviruses. We have examined two novel mechanisms that could regulate NIa-Pro activity. Firstly, the influence of VPg domain on the proteolytic activity of NIa-Pro was investigated. It was shown that the turnover number of the protease increases when these two domains interact ( cis : two-fold; trans : seven-fold) with each other. Secondly, the protease activity of NIa-Pro could also be modulated by phosphorylation at Ser129. A mutation of this residue either to aspartate (phosphorylation-mimic) or alanine (phosphorylation-deficient) drastically reduces the protease activity. Based on these observations and molecular modeling studies, we propose that interaction with VPg as well as phosphorylation of Ser129 could relay a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22099968</pmid><doi>10.1016/j.virol.2011.10.009</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0042-6822 |
| ispartof | Virology (New York, N.Y.), 2012-01, Vol.422 (2), p.254-264 |
| issn | 0042-6822 1096-0341 |
| language | eng |
| recordid | cdi_osti_scitechconnect_22149253 |
| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | 60 APPLIED LIFE SCIENCES ALANINES Base Sequence Chromatography, Thin Layer Circular Dichroism CONFORMATIONAL CHANGES Endopeptidases - genetics Endopeptidases - metabolism Gene Expression Regulation, Viral - physiology Genome, Viral HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY HPLC-based protease assay Infectious Disease Molecular modeling Mutation Nuclear Inclusion protein-a protease (NIa-Pro) Pepper Vein Banding Virus (PVBV) PHOSPHORYLATION PHOSPHOTRANSFERASES Potyviridae Potyvirus - metabolism RNA, Viral - chemistry RNA, Viral - genetics RNA, Viral - metabolism Spectrometry, Fluorescence VEINS Viral Protein genome-linked (VPg) Viral Proteins - genetics Viral Proteins - metabolism VIRUSES VPg-Pro |
| title | Functional regulation of PVBV Nuclear Inclusion protein-a protease activity upon interaction with Viral Protein genome-linked and phosphorylation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T16%3A18%3A57IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Functional%20regulation%20of%20PVBV%20Nuclear%20Inclusion%20protein-a%20protease%20activity%20upon%20interaction%20with%20Viral%20Protein%20genome-linked%20and%20phosphorylation&rft.jtitle=Virology%20(New%20York,%20N.Y.)&rft.au=Mathur,%20C&rft.date=2012-01-20&rft.volume=422&rft.issue=2&rft.spage=254&rft.epage=264&rft.pages=254-264&rft.issn=0042-6822&rft.eissn=1096-0341&rft_id=info:doi/10.1016/j.virol.2011.10.009&rft_dat=%3Cproquest_osti_%3E918055005%3C/proquest_osti_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=913442634&rft_id=info:pmid/22099968&rft_els_id=1_s2_0_S0042682211004788&rfr_iscdi=true |