Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

MtPM25 is an atypical hydrophobic late embryogenesis‐abundant protein that dissociates cold and desiccation‐aggregated proteins

MtPM25 is an atypical hydrophobic late embryogenesis‐abundant protein that dissociates cold and... ABSTRACT Late embryogenesis‐abundant (LEA) proteins are one of the components involved in desiccation tolerance (DT) by maintaining cellular structures in the dry state. Among them, MtPM25, a member of the group 5 is specifically associated with DT in Medicago truncatula seeds. Its function is unknown and its classification as a LEA protein remains elusive. Here, evidence is provided that MtPM25 is a hydrophobic, intrinsically disordered protein that shares the characteristics of canonical LEA proteins. Screening protective activities by testing various substrates against freezing, heating and drying indicates that MtPM25 is unable to protect membranes but able to prevent aggregation of proteins during stress. Prevention of aggregation was also found for the water soluble proteome of desiccation‐sensitive radicles. This inhibition was significantly higher than that of MtEM6, one of the most hydrophilic LEA protein associated with DT. Moreover, when added after the stress treatment, MtPM25 is able to rapidly dissolve aggregates in a non‐specific manner. Sorption isotherms show that when it is unstructured, MtPM25 absorbs up to threefold more water than MtEM6. MtPM25 is likely to act as a protective molecule during drying and plays an additional role as a repair mechanism compared with other LEA proteins. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Cell & Environment Wiley

MtPM25 is an atypical hydrophobic late embryogenesis‐abundant protein that dissociates cold and desiccation‐aggregated proteins

Loading next page...
 
/lp/wiley/mtpm25-is-an-atypical-hydrophobic-late-embryogenesis-abundant-protein-SRO5r2olFQ

References (40)

Publisher
Wiley
Copyright
© 2010 Blackwell Publishing Ltd
ISSN
0140-7791
eISSN
1365-3040
DOI
10.1111/j.1365-3040.2009.02093.x
pmid
20002332
Publisher site
See Article on Publisher Site

Abstract

ABSTRACT Late embryogenesis‐abundant (LEA) proteins are one of the components involved in desiccation tolerance (DT) by maintaining cellular structures in the dry state. Among them, MtPM25, a member of the group 5 is specifically associated with DT in Medicago truncatula seeds. Its function is unknown and its classification as a LEA protein remains elusive. Here, evidence is provided that MtPM25 is a hydrophobic, intrinsically disordered protein that shares the characteristics of canonical LEA proteins. Screening protective activities by testing various substrates against freezing, heating and drying indicates that MtPM25 is unable to protect membranes but able to prevent aggregation of proteins during stress. Prevention of aggregation was also found for the water soluble proteome of desiccation‐sensitive radicles. This inhibition was significantly higher than that of MtEM6, one of the most hydrophilic LEA protein associated with DT. Moreover, when added after the stress treatment, MtPM25 is able to rapidly dissolve aggregates in a non‐specific manner. Sorption isotherms show that when it is unstructured, MtPM25 absorbs up to threefold more water than MtEM6. MtPM25 is likely to act as a protective molecule during drying and plays an additional role as a repair mechanism compared with other LEA proteins.

Journal

Plant Cell & EnvironmentWiley

Published: Mar 1, 2010

There are no references for this article.