Prediction of functions for two LEA proteins from mung bean

LEA (late embryogenesis abundant) proteins are associated with tolerance to water stress resulting from desiccation and cold shock. Although various functions have been proposed to LEA proteins, their precise role is not fully defined. In silico analysis of the amino acid sequence of two LEA protein...

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Detalles Bibliográficos
Autores principales: Rajesh, Subramanian, Manickam, Ayyanar
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics Publishing Group 2006
Materias:
Hypothesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891666/
https://www.ncbi.nlm.nih.gov/pubmed/17597874
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author Rajesh, Subramanian
Manickam, Ayyanar
author_facet Rajesh, Subramanian
Manickam, Ayyanar
author_sort Rajesh, Subramanian
collection PubMed
description LEA (late embryogenesis abundant) proteins are associated with tolerance to water stress resulting from desiccation and cold shock. Although various functions have been proposed to LEA proteins, their precise role is not fully defined. In silico analysis of the amino acid sequence of two LEA proteins (early methionine-labeled Vigna, EMV) from the tropical legume crop, Vigna radiata identified a 20 residues motif ‘GGQTRKQQLGSEGYHEMGRK’ characteristic to group 1 LEA proteins. Structural analyses hypothesize these proteins to function like DNA/RNA binding proteins in protecting macromolecules/ membrane stabilization at the time of dehydration process.
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spelling pubmed-18916662007-06-27 Prediction of functions for two LEA proteins from mung bean Rajesh, Subramanian Manickam, Ayyanar Bioinformation Hypothesis LEA (late embryogenesis abundant) proteins are associated with tolerance to water stress resulting from desiccation and cold shock. Although various functions have been proposed to LEA proteins, their precise role is not fully defined. In silico analysis of the amino acid sequence of two LEA proteins (early methionine-labeled Vigna, EMV) from the tropical legume crop, Vigna radiata identified a 20 residues motif ‘GGQTRKQQLGSEGYHEMGRK’ characteristic to group 1 LEA proteins. Structural analyses hypothesize these proteins to function like DNA/RNA binding proteins in protecting macromolecules/ membrane stabilization at the time of dehydration process. Biomedical Informatics Publishing Group 2006-04-16 /pmc/articles/PMC1891666/ /pubmed/17597874 Text en © 2006 Biomedical Informatics Publishing Group This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Rajesh, Subramanian
Manickam, Ayyanar
Prediction of functions for two LEA proteins from mung bean
title Prediction of functions for two LEA proteins from mung bean
title_full Prediction of functions for two LEA proteins from mung bean
title_fullStr Prediction of functions for two LEA proteins from mung bean
title_full_unstemmed Prediction of functions for two LEA proteins from mung bean
title_short Prediction of functions for two LEA proteins from mung bean
title_sort prediction of functions for two lea proteins from mung bean
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891666/
https://www.ncbi.nlm.nih.gov/pubmed/17597874
work_keys_str_mv AT rajeshsubramanian predictionoffunctionsfortwoleaproteinsfrommungbean
AT manickamayyanar predictionoffunctionsfortwoleaproteinsfrommungbean

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