The LEA proteins and trehalose loving couple: a step forward in anhydrobiotic engineering

Adaptation to desiccation tolerance or anhydrobiosis has puzzled scientists for more than 300 years. Over the last few decades, considerable emphasis has been placed on understanding the role of two key molecules involved in anhydrobiosis: a peculiar disaccharide named trehalose and the hydrophilic...

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Bibliographic Details
Published inBiochemical journal Vol. 410; no. 2; p. e1
Main Author Iturriaga, Gabriel
Format Journal Article
LanguageEnglish
Published England 01.03.2008
Subjects
Antigens, Surface - metabolism
Biomedical Engineering - methods
Biomedical Engineering - trends
Computational Biology
Membrane Glycoproteins - metabolism
Models, Biological
Trehalose - metabolism
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Summary:Adaptation to desiccation tolerance or anhydrobiosis has puzzled scientists for more than 300 years. Over the last few decades, considerable emphasis has been placed on understanding the role of two key molecules involved in anhydrobiosis: a peculiar disaccharide named trehalose and the hydrophilic LEA (Late Embryogenesis Abundant) proteins. In an article published in the Biochemical Journal in 2005, Alan Tunnacliffe and colleagues found that LEA proteins (alone, or more so in combination with trehalose) can protect stress-sensitive enzymes, such as citrate synthase and lactate dehydrogenase, from aggregation due to desiccation and freezing. Upon heat-stress, however, LEA proteins alone cannot prevent these enzymes from aggregating unless trehalose is present. This is the first report that LEA proteins can act as 'molecular shields' to prevent aggregation-induced cell damage due to water loss.
ISSN:1470-8728
DOI:10.1042/bj20071633