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Temperature dependent N-glycosylation of plasma membrane heat shock protein Hsp30p in Saccharomyces cerevisiae.

Abstract：

:The HSP30 gene of the budding yeast Saccharomyces cerevisiae encodes a seven-transmembrane heat shock protein expressed in response to various types of stress including heat shock. Although Hsp30p contains a potential N-glycosylation consensus sequence (Asn(2)-Asp(3)-Thr(4)), whether it is actually N-glycosylated has not been verified. Here we demonstrate that N-glycosylation is induced at Asn(2) of Hsp30p by severe heat shock, ethanol stress, and acetic acid stress. Mild heat shock and glucose depletion induced the expression but not N-glycosylation of Hsp30p, indicating the N-glycosylation to be dependent on temperature and environmental conditions. N-glycosylation did not affect on the intracellular localization of Hsp30p but its physiological role under severe heat shock conditions. Since limited information is available on stress-responsive or condition-induced N-glycosylation, our findings provide new insight into the regulation of cellular stress response in yeast.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kamo K,Takabatake A,Inoue Y,Izawa S

doi

10.1016/j.bbrc.2012.02.126

subject

Has Abstract

pub_date

2012-03-30 00:00:00

pages

119-23

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(12)00385-3

journal_volume

420

pub_type

杂志文章

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