A proteomic analysis of oligo(dT)-bound mRNP containing oxidative stress-induced Arabidopsis thaliana RNA-binding proteins ATGRP7 and ATGRP8

Schmidt, F. , Marnef, A. , Cheung, M.-K. , Wilson, I. D. , Hancock, J. T. , Staiger, D. and Ladomery, M. (2010) A proteomic analysis of oligo(dT)-bound mRNP containing oxidative stress-induced Arabidopsis thaliana RNA-binding proteins ATGRP7 and ATGRP8. Molecular Biology Reports, 37 (2). pp. 839-845. ISSN 0301-4851

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Publisher's URL: http://dx.doi.org/10.1007/s11033-009-9636-x

Abstract

Plants are highly adapted to respond to a range of environmental stresses commonly by altering their gene expression and metabolism as a result of cell signalling which may be mediated by reactive oxygen species. The glycine-rich RNA-binding proteins ATGRP7 and ATGRP8 were rapidly upregulated in response to peroxide-induced oxidative stress and were amongst the most abundant RNA binding proteins isolated by oligo(dT) chromatography. The oligo(dT)-bound mRNP complexes were analysed proteomically, and were seen to contain potential isoforms of the ATGRP proteins; other proteins that contain an RNA Recognition Motif (RRM); and chloroplast RNA binding proteins. These findings suggest that ATGRP proteins have an evolutionarily conserved function in the regulation of gene expression at the posttranscriptional level in response to environmental stress.

Item Type:Article
Uncontrolled Keywords:RNA binding proteins, RNA recognition motif, ATGRP7, ATGRP8, oxidative stress, mRNP particles, oligo(dT), chromatography
Faculty/Department:Faculty of Health and Life Sciences > Department of Applied Sciences
~Pre-2010 Faculty Structure > Health and Life Sciences > School of Life Sciences > Centre for Research in Plant and Environmental Science
~Pre-2012 Faculty Structure > Faculty of Health and Life Sciences > Department of Applied Sciences
ID Code:8276
Deposited By: Dr J. Hancock
Deposited On:09 Jul 2010 09:06
Last Modified:28 Feb 2013 10:27

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