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Structure of RNA-interacting Cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants
Soil salinity problems are widespread around the globe with increased risk of spreading over the years. The fungus Piriformospora indica, identified in Indian Thar desert, colonizes the roots of monocotyledon plants and provides resistance towards biotic as well as abiotic stress conditions. We have...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3801112/ https://www.ncbi.nlm.nih.gov/pubmed/24141523 http://dx.doi.org/10.1038/srep03001 |
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author | Trivedi, Dipesh Kumar Bhatt, Harshesh Pal, Ravi Kant Tuteja, Renu Garg, Bharti Johri, Atul Kumar Bhavesh, Neel Sarovar Tuteja, Narendra |
author_facet | Trivedi, Dipesh Kumar Bhatt, Harshesh Pal, Ravi Kant Tuteja, Renu Garg, Bharti Johri, Atul Kumar Bhavesh, Neel Sarovar Tuteja, Narendra |
author_sort | Trivedi, Dipesh Kumar |
collection | PubMed |
description | Soil salinity problems are widespread around the globe with increased risk of spreading over the years. The fungus Piriformospora indica, identified in Indian Thar desert, colonizes the roots of monocotyledon plants and provides resistance towards biotic as well as abiotic stress conditions. We have identified a cyclophilin A-like protein from P. indica (PiCypA), which shows higher expression levels during salinity stress. The transgenic tobacco plants overexpressing PiCypA develop osmotic tolerance and exhibit normal growth under osmotic stress conditions. The crystal structure and NMR spectroscopy of PiCypA show a canonical cyclophilin like fold exhibiting a novel RNA binding activity. The RNA binding activity of the protein and identification of the key residues involved in the RNA recognition is unique for this class of protein. Here, we demonstrate for the first time a direct evidence of countering osmotic stress tolerance in plant by genetic modification using a P. indica gene. |
format | Online Article Text |
id | pubmed-3801112 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-38011122013-10-21 Structure of RNA-interacting Cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants Trivedi, Dipesh Kumar Bhatt, Harshesh Pal, Ravi Kant Tuteja, Renu Garg, Bharti Johri, Atul Kumar Bhavesh, Neel Sarovar Tuteja, Narendra Sci Rep Article Soil salinity problems are widespread around the globe with increased risk of spreading over the years. The fungus Piriformospora indica, identified in Indian Thar desert, colonizes the roots of monocotyledon plants and provides resistance towards biotic as well as abiotic stress conditions. We have identified a cyclophilin A-like protein from P. indica (PiCypA), which shows higher expression levels during salinity stress. The transgenic tobacco plants overexpressing PiCypA develop osmotic tolerance and exhibit normal growth under osmotic stress conditions. The crystal structure and NMR spectroscopy of PiCypA show a canonical cyclophilin like fold exhibiting a novel RNA binding activity. The RNA binding activity of the protein and identification of the key residues involved in the RNA recognition is unique for this class of protein. Here, we demonstrate for the first time a direct evidence of countering osmotic stress tolerance in plant by genetic modification using a P. indica gene. Nature Publishing Group 2013-10-21 /pmc/articles/PMC3801112/ /pubmed/24141523 http://dx.doi.org/10.1038/srep03001 Text en Copyright © 2013, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-nd/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial- NoDerivs 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/ |
spellingShingle | Article Trivedi, Dipesh Kumar Bhatt, Harshesh Pal, Ravi Kant Tuteja, Renu Garg, Bharti Johri, Atul Kumar Bhavesh, Neel Sarovar Tuteja, Narendra Structure of RNA-interacting Cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants |
title | Structure of RNA-interacting Cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants |
title_full | Structure of RNA-interacting Cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants |
title_fullStr | Structure of RNA-interacting Cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants |
title_full_unstemmed | Structure of RNA-interacting Cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants |
title_short | Structure of RNA-interacting Cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants |
title_sort | structure of rna-interacting cyclophilin a-like protein from piriformospora indica that provides salinity-stress tolerance in plants |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3801112/ https://www.ncbi.nlm.nih.gov/pubmed/24141523 http://dx.doi.org/10.1038/srep03001 |
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