Identification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle protein
Autor(a) principal: | |
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Data de Publicação: | 2004 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1016/j.virol.2003.09.038 http://www.locus.ufv.br/handle/123456789/14310 |
Resumo: | Despite extensive studies in plant virus – host interactions, the molecular mechanisms of geminivirus movement and interactions with host components remain largely unknown. A tomato kinase protein and its soybean homolog were found to interact specifically with the nuclear shuttle protein (NSP) of Tomato golden mosaic virus (TGMV) and Tomato crinkle leaf yellows virus (TCrLYV) through yeast two-hybrid screening and in vitro protein binding assays. These proteins, designated LeNIK (Lycopersicon esculentum NSP-Interacting Kinase) and GmNIK (Glycine max NIK), belong to the LRR-RLK (leucine rich-repeat receptor-like kinase) family that is involved in plant developmental processes and/or resistance response. As such, NIK is structurally organized into characteristic domains, including a serine/threonine kinase domain with a nucleotide binding site at the C-terminal region, an internal transmembrane segment and leucine-rich repeats (LRR) at the N- terminal portion. The potential significance of the NSP – NIK interaction is discussed. |
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Mariano, Andrea C.Andrade, Maxuel O.Santos, Anésia A.Carolino, Sonia M.B.Oliveira, Marli L.Baracat-Pereira, Maria CristinaBrommonshenkel, Sergio H.Fontes, Elizabeth P.B.2017-12-04T10:29:58Z2017-12-04T10:29:58Z2004-09-2600426822https://doi.org/10.1016/j.virol.2003.09.038http://www.locus.ufv.br/handle/123456789/14310Despite extensive studies in plant virus – host interactions, the molecular mechanisms of geminivirus movement and interactions with host components remain largely unknown. A tomato kinase protein and its soybean homolog were found to interact specifically with the nuclear shuttle protein (NSP) of Tomato golden mosaic virus (TGMV) and Tomato crinkle leaf yellows virus (TCrLYV) through yeast two-hybrid screening and in vitro protein binding assays. These proteins, designated LeNIK (Lycopersicon esculentum NSP-Interacting Kinase) and GmNIK (Glycine max NIK), belong to the LRR-RLK (leucine rich-repeat receptor-like kinase) family that is involved in plant developmental processes and/or resistance response. As such, NIK is structurally organized into characteristic domains, including a serine/threonine kinase domain with a nucleotide binding site at the C-terminal region, an internal transmembrane segment and leucine-rich repeats (LRR) at the N- terminal portion. The potential significance of the NSP – NIK interaction is discussed.engVirologyVolume 318, Issue 1, Pages 24-31, January 2004Tomato kinase proteinGeminivirusNuclear shuttle proteinIdentification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle proteininfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfinfo:eu-repo/semantics/openAccessreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINAL1-s2.0-S0042682203007414-main.pdf1-s2.0-S0042682203007414-main.pdftexto completoapplication/pdf883243https://locus.ufv.br//bitstream/123456789/14310/1/1-s2.0-S0042682203007414-main.pdf3aca0000ef40b59b95b29e2589174aa9MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/14310/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAIL1-s2.0-S0042682203007414-main.pdf.jpg1-s2.0-S0042682203007414-main.pdf.jpgIM Thumbnailimage/jpeg6243https://locus.ufv.br//bitstream/123456789/14310/3/1-s2.0-S0042682203007414-main.pdf.jpg7d5ddb80c6854cd900c14e80da014d61MD53123456789/143102018-04-17 11:06:58.944oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-04-17T14:06:58LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Identification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle protein |
title |
Identification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle protein |
spellingShingle |
Identification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle protein Mariano, Andrea C. Tomato kinase protein Geminivirus Nuclear shuttle protein |
title_short |
Identification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle protein |
title_full |
Identification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle protein |
title_fullStr |
Identification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle protein |
title_full_unstemmed |
Identification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle protein |
title_sort |
Identification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle protein |
author |
Mariano, Andrea C. |
author_facet |
Mariano, Andrea C. Andrade, Maxuel O. Santos, Anésia A. Carolino, Sonia M.B. Oliveira, Marli L. Baracat-Pereira, Maria Cristina Brommonshenkel, Sergio H. Fontes, Elizabeth P.B. |
author_role |
author |
author2 |
Andrade, Maxuel O. Santos, Anésia A. Carolino, Sonia M.B. Oliveira, Marli L. Baracat-Pereira, Maria Cristina Brommonshenkel, Sergio H. Fontes, Elizabeth P.B. |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Mariano, Andrea C. Andrade, Maxuel O. Santos, Anésia A. Carolino, Sonia M.B. Oliveira, Marli L. Baracat-Pereira, Maria Cristina Brommonshenkel, Sergio H. Fontes, Elizabeth P.B. |
dc.subject.pt-BR.fl_str_mv |
Tomato kinase protein Geminivirus Nuclear shuttle protein |
topic |
Tomato kinase protein Geminivirus Nuclear shuttle protein |
description |
Despite extensive studies in plant virus – host interactions, the molecular mechanisms of geminivirus movement and interactions with host components remain largely unknown. A tomato kinase protein and its soybean homolog were found to interact specifically with the nuclear shuttle protein (NSP) of Tomato golden mosaic virus (TGMV) and Tomato crinkle leaf yellows virus (TCrLYV) through yeast two-hybrid screening and in vitro protein binding assays. These proteins, designated LeNIK (Lycopersicon esculentum NSP-Interacting Kinase) and GmNIK (Glycine max NIK), belong to the LRR-RLK (leucine rich-repeat receptor-like kinase) family that is involved in plant developmental processes and/or resistance response. As such, NIK is structurally organized into characteristic domains, including a serine/threonine kinase domain with a nucleotide binding site at the C-terminal region, an internal transmembrane segment and leucine-rich repeats (LRR) at the N- terminal portion. The potential significance of the NSP – NIK interaction is discussed. |
publishDate |
2004 |
dc.date.issued.fl_str_mv |
2004-09-26 |
dc.date.accessioned.fl_str_mv |
2017-12-04T10:29:58Z |
dc.date.available.fl_str_mv |
2017-12-04T10:29:58Z |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
format |
article |
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publishedVersion |
dc.identifier.uri.fl_str_mv |
https://doi.org/10.1016/j.virol.2003.09.038 http://www.locus.ufv.br/handle/123456789/14310 |
dc.identifier.issn.none.fl_str_mv |
00426822 |
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00426822 |
url |
https://doi.org/10.1016/j.virol.2003.09.038 http://www.locus.ufv.br/handle/123456789/14310 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
Volume 318, Issue 1, Pages 24-31, January 2004 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
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Virology |
publisher.none.fl_str_mv |
Virology |
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