Identification of a novel receptor-like protein kinase that interacts with a geminivirus nuclear shuttle protein

Detalhes bibliográficos
Autor(a) principal: Mariano, Andrea C.
Data de Publicação: 2004
Outros Autores: Andrade, Maxuel O., Santos, Anésia A., Carolino, Sonia M.B., Oliveira, Marli L., Baracat-Pereira, Maria Cristina, Brommonshenkel, Sergio H., Fontes, Elizabeth P.B.
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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spelling 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:123456789/14310Tk9URTogUExBQ0UgWU9VUiBPV04gTElDRU5TRSBIRVJFClRoaXMgc2FtcGxlIGxpY2Vuc2UgaXMgcHJvdmlkZWQgZm9yIGluZm9ybWF0aW9uYWwgcHVycG9zZXMgb25seS4KCk5PTi1FWENMVVNJVkUgRElTVFJJQlVUSU9OIExJQ0VOU0UKCkJ5IHNpZ25pbmcgYW5kIHN1Ym1pdHRpbmcgdGhpcyBsaWNlbnNlLCB5b3UgKHRoZSBhdXRob3Iocykgb3IgY29weXJpZ2h0Cm93bmVyKSBncmFudHMgdG8gRFNwYWNlIFVuaXZlcnNpdHkgKERTVSkgdGhlIG5vbi1leGNsdXNpdmUgcmlnaHQgdG8gcmVwcm9kdWNlLAp0cmFuc2xhdGUgKGFzIGRlZmluZWQgYmVsb3cpLCBhbmQvb3IgZGlzdHJpYnV0ZSB5b3VyIHN1Ym1pc3Npb24gKGluY2x1ZGluZwp0aGUgYWJzdHJhY3QpIHdvcmxkd2lkZSBpbiBwcmludCBhbmQgZWxlY3Ryb25pYyBmb3JtYXQgYW5kIGluIGFueSBtZWRpdW0sCmluY2x1ZGluZyBidXQgbm90IGxpbWl0ZWQgdG8gYXVkaW8gb3IgdmlkZW8uCgpZb3UgYWdyZWUgdGhhdCBEU1UgbWF5LCB3aXRob3V0IGNoYW5naW5nIHRoZSBjb250ZW50LCB0cmFuc2xhdGUgdGhlCnN1Ym1pc3Npb24gdG8gYW55IG1lZGl1bSBvciBmb3JtYXQgZm9yIHRoZSBwdXJwb3NlIG9mIHByZXNlcnZhdGlvbi4KCllvdSBhbHNvIGFncmVlIHRoYXQgRFNVIG1heSBrZWVwIG1vcmUgdGhhbiBvbmUgY29weSBvZiB0aGlzIHN1Ym1pc3Npb24gZm9yCnB1cnBvc2VzIG9mIHNlY3VyaXR5LCBiYWNrLXVwIGFuZCBwcmVzZXJ2YXRpb24uCgpZb3UgcmVwcmVzZW50IHRoYXQgdGhlIHN1Ym1pc3Npb24gaXMgeW91ciBvcmlnaW5hbCB3b3JrLCBhbmQgdGhhdCB5b3UgaGF2ZQp0aGUgcmlnaHQgdG8gZ3JhbnQgdGhlIHJpZ2h0cyBjb250YWluZWQgaW4gdGhpcyBsaWNlbnNlLiBZb3UgYWxzbyByZXByZXNlbnQKdGhhdCB5b3VyIHN1Ym1pc3Npb24gZG9lcyBub3QsIHRvIHRoZSBiZXN0IG9mIHlvdXIga25vd2xlZGdlLCBpbmZyaW5nZSB1cG9uCmFueW9uZSdzIGNvcHlyaWdodC4KCklmIHRoZSBzdWJtaXNzaW9uIGNvbnRhaW5zIG1hdGVyaWFsIGZvciB3aGljaCB5b3UgZG8gbm90IGhvbGQgY29weXJpZ2h0LAp5b3UgcmVwcmVzZW50IHRoYXQgeW91IGhhdmUgb2J0YWluZWQgdGhlIHVucmVzdHJpY3RlZCBwZXJtaXNzaW9uIG9mIHRoZQpjb3B5cmlnaHQgb3duZXIgdG8gZ3JhbnQgRFNVIHRoZSByaWdodHMgcmVxdWlyZWQgYnkgdGhpcyBsaWNlbnNlLCBhbmQgdGhhdApzdWNoIHRoaXJkLXBhcnR5IG93bmVkIG1hdGVyaWFsIGlzIGNsZWFybHkgaWRlbnRpZmllZCBhbmQgYWNrbm93bGVkZ2VkCndpdGhpbiB0aGUgdGV4dCBvciBjb250ZW50IG9mIHRoZSBzdWJtaXNzaW9uLgoKSUYgVEhFIFNVQk1JU1NJT04gSVMgQkFTRUQgVVBPTiBXT1JLIFRIQVQgSEFTIEJFRU4gU1BPTlNPUkVEIE9SIFNVUFBPUlRFRApCWSBBTiBBR0VOQ1kgT1IgT1JHQU5JWkFUSU9OIE9USEVSIFRIQU4gRFNVLCBZT1UgUkVQUkVTRU5UIFRIQVQgWU9VIEhBVkUKRlVMRklMTEVEIEFOWSBSSUdIVCBPRiBSRVZJRVcgT1IgT1RIRVIgT0JMSUdBVElPTlMgUkVRVUlSRUQgQlkgU1VDSApDT05UUkFDVCBPUiBBR1JFRU1FTlQuCgpEU1Ugd2lsbCBjbGVhcmx5IGlkZW50aWZ5IHlvdXIgbmFtZShzKSBhcyB0aGUgYXV0aG9yKHMpIG9yIG93bmVyKHMpIG9mIHRoZQpzdWJtaXNzaW9uLCBhbmQgd2lsbCBub3QgbWFrZSBhbnkgYWx0ZXJhdGlvbiwgb3RoZXIgdGhhbiBhcyBhbGxvd2VkIGJ5IHRoaXMKbGljZW5zZSwgdG8geW91ciBzdWJtaXNzaW9uLgo=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
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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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
identifier_str_mv 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
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dc.relation.ispartofseries.pt-BR.fl_str_mv Volume 318, Issue 1, Pages 24-31, January 2004
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.publisher.none.fl_str_mv Virology
publisher.none.fl_str_mv Virology
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