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Published online ahead of print on 21 April 2009 as doi:10.1099/mic.0.025981-0
Microbiology 2009;155:2021.

Microbiology (2009), DOI 10.1099/mic.0.025981-0
© 2009 Society for General Microbiology

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Microbiology 0 (2009), mic.0.025981; DOI  10.1099/mic.0.025981-0
© 2009 Society for General Microbiology


Small heat-shock protein Hsp12 contributes to yeast tolerance to freezing stress

A. Pacheco, C. Pereira, M. J. Almeida and M. J. Sousa1

UNIVERSITY OF MINHO

ABSTRACT

HSP12 gene encodes one of the two major small heat shock proteins of Saccharomyces cerevisiae and is induced under different conditions, such as low and high temperatures, osmotic or oxidative stress and high sugar or ethanol concentrations. However, few studies could demonstrate any correlation between HSP12 deletion or overexpression and a phenotype of sensitivity/resistance, making it difficult to attribute a role for Hsp12p under several of these stress conditions. Herein, we investigated the possible role of Hsp12p in yeast freezing tolerance. Contrary to what would be expected, the hsp12 null mutant when subjected to prolonged storage at -20 °C showed an increased resistance to freezing when compared with the isogenic wild type strain. Because the mutant strain displayed a higher intracellular trehalose concentration than the wild type, which could mask the effect of manipulating HSP12, we overexpressed HSP12 gene in a trehalose-6-phosphate synthase (TPS1) null mutant. {Delta}tps1 strain overexpressing HSP12 showed an increase in resistance to freezing storage, indicating that Hsp12p plays a role in freezing tolerance in a way that seems to be interchangeable with trehalose. In addition, we show that overexpression of HSP12 in this {Delta}tps1 strain also increased resistance to heat shock and that absence of HSP12 compromises the ability of yeast cells to accumulate high levels of trehalose in response to a mild heat stress.

1 E-mail: mjsousa{at}bio.uminho.pt







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