Evolutionary and structural aspects of Solanaceae RNases T2
Autor(a) principal: | |
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Data de Publicação: | 2023 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/266582 |
Resumo: | Plant RNases T2 are involved in several physiological and developmental processes, including inorganic phosphate starvation, senescence, wounding, defense against pathogens, and the self-incompatibility system. Solanaceae RNases form three main clades, one composed exclusively of S-RNases and two that include S-like RNases. We identified several positively selected amino acids located in highly flexible regions of these molecules, mainly close to the B1 and B2 substrate-binding sites in S-like RNases and the hypervariable regions of S-RNases. These differences between S- and S-like RNases in the flexibility of amino acids in substrate-binding regions are essential to understand the RNA-binding process. For example, in the S-like RNase NT, two positively selected amino acid residues (Tyr156 and Asn134) are located at the most flexible sites on the molecular surface. RNase NT is induced in response to tobacco mosaic virus infection; these sites may thus be regions of interaction with pathogen proteins or viral RNA. Differential selective pressures acting on plant ribonucleases have increased amino acid variability and, consequently, structural differences within and among S-like RNases and S-RNases that seem to be essential for these proteins play different functions. |
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Thompson, Claudia ElizabethCorrêa, Lauís BrisolaraThompson, Helen NathaliaStassen, Hubert KarlFreitas, Loreta Brandão de2023-11-04T03:31:52Z20231415-4757http://hdl.handle.net/10183/266582001170544Plant RNases T2 are involved in several physiological and developmental processes, including inorganic phosphate starvation, senescence, wounding, defense against pathogens, and the self-incompatibility system. Solanaceae RNases form three main clades, one composed exclusively of S-RNases and two that include S-like RNases. We identified several positively selected amino acids located in highly flexible regions of these molecules, mainly close to the B1 and B2 substrate-binding sites in S-like RNases and the hypervariable regions of S-RNases. These differences between S- and S-like RNases in the flexibility of amino acids in substrate-binding regions are essential to understand the RNA-binding process. For example, in the S-like RNase NT, two positively selected amino acid residues (Tyr156 and Asn134) are located at the most flexible sites on the molecular surface. RNase NT is induced in response to tobacco mosaic virus infection; these sites may thus be regions of interaction with pathogen proteins or viral RNA. Differential selective pressures acting on plant ribonucleases have increased amino acid variability and, consequently, structural differences within and among S-like RNases and S-RNases that seem to be essential for these proteins play different functions.application/pdfengGenetics and molecular biology. Ribeirão Preto. Vol. 46, no. 1 suppl. 1 (2023), e20220115, 15 p.Ribonucleases T2SolanaceaeFunctional diversificationStructural biologyEvolutionary and structural aspects of Solanaceae RNases T2info:eu-repo/semantics/articleinfo:eu-repo/semantics/otherinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSTEXT001170544.pdf.txt001170544.pdf.txtExtracted Texttext/plain66700http://www.lume.ufrgs.br/bitstream/10183/266582/2/001170544.pdf.txt7129a6d98fb3061c7bed371c8a8a084eMD52ORIGINAL001170544.pdfTexto completo (inglês)application/pdf8793813http://www.lume.ufrgs.br/bitstream/10183/266582/1/001170544.pdf3dba40e7ae0349b29c050d3ca4e9a2e9MD5110183/2665822024-05-23 06:42:36.837216oai:www.lume.ufrgs.br:10183/266582Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2024-05-23T09:42:36Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.fl_str_mv |
Evolutionary and structural aspects of Solanaceae RNases T2 |
title |
Evolutionary and structural aspects of Solanaceae RNases T2 |
spellingShingle |
Evolutionary and structural aspects of Solanaceae RNases T2 Thompson, Claudia Elizabeth Ribonucleases T2 Solanaceae Functional diversification Structural biology |
title_short |
Evolutionary and structural aspects of Solanaceae RNases T2 |
title_full |
Evolutionary and structural aspects of Solanaceae RNases T2 |
title_fullStr |
Evolutionary and structural aspects of Solanaceae RNases T2 |
title_full_unstemmed |
Evolutionary and structural aspects of Solanaceae RNases T2 |
title_sort |
Evolutionary and structural aspects of Solanaceae RNases T2 |
author |
Thompson, Claudia Elizabeth |
author_facet |
Thompson, Claudia Elizabeth Corrêa, Lauís Brisolara Thompson, Helen Nathalia Stassen, Hubert Karl Freitas, Loreta Brandão de |
author_role |
author |
author2 |
Corrêa, Lauís Brisolara Thompson, Helen Nathalia Stassen, Hubert Karl Freitas, Loreta Brandão de |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Thompson, Claudia Elizabeth Corrêa, Lauís Brisolara Thompson, Helen Nathalia Stassen, Hubert Karl Freitas, Loreta Brandão de |
dc.subject.por.fl_str_mv |
Ribonucleases T2 Solanaceae |
topic |
Ribonucleases T2 Solanaceae Functional diversification Structural biology |
dc.subject.eng.fl_str_mv |
Functional diversification Structural biology |
description |
Plant RNases T2 are involved in several physiological and developmental processes, including inorganic phosphate starvation, senescence, wounding, defense against pathogens, and the self-incompatibility system. Solanaceae RNases form three main clades, one composed exclusively of S-RNases and two that include S-like RNases. We identified several positively selected amino acids located in highly flexible regions of these molecules, mainly close to the B1 and B2 substrate-binding sites in S-like RNases and the hypervariable regions of S-RNases. These differences between S- and S-like RNases in the flexibility of amino acids in substrate-binding regions are essential to understand the RNA-binding process. For example, in the S-like RNase NT, two positively selected amino acid residues (Tyr156 and Asn134) are located at the most flexible sites on the molecular surface. RNase NT is induced in response to tobacco mosaic virus infection; these sites may thus be regions of interaction with pathogen proteins or viral RNA. Differential selective pressures acting on plant ribonucleases have increased amino acid variability and, consequently, structural differences within and among S-like RNases and S-RNases that seem to be essential for these proteins play different functions. |
publishDate |
2023 |
dc.date.accessioned.fl_str_mv |
2023-11-04T03:31:52Z |
dc.date.issued.fl_str_mv |
2023 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/other |
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info:eu-repo/semantics/publishedVersion |
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article |
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publishedVersion |
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http://hdl.handle.net/10183/266582 |
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1415-4757 |
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001170544 |
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http://hdl.handle.net/10183/266582 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.pt_BR.fl_str_mv |
Genetics and molecular biology. Ribeirão Preto. Vol. 46, no. 1 suppl. 1 (2023), e20220115, 15 p. |
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info:eu-repo/semantics/openAccess |
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openAccess |
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