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In vivo aggregation of a single enzyme limits growth of Escherichia coli at elevated temperatures
Author(s) -
Gur Eyal,
Biran Dvora,
Gazit Ehud,
Ron Eliora Z.
Publication year - 2002
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2002.03257.x
Subject(s) - escherichia coli , in vivo , biology , enzyme , protein aggregation , biochemistry , methionine , bacteria , denaturation (fissile materials) , in vitro , bacterial growth , biophysics , amino acid , chemistry , gene , genetics , microbiology and biotechnology , nuclear chemistry
Summary The formation of protein aggregates is associated with unfolding and denaturation of proteins. Recent studies have indicated that, in Escherichia coli , cellular proteins tend to aggregate when the bacteria are exposed to thermal stress. Here, we show that the aggregation of one single E . coli cytoplasmic protein limits growth at elevated temperatures in minimal media. Homoserine trans ‐succinylase (HTS), the first enzyme in the methionine biosynthetic pathway, aggregates at temperatures higher than 44°C in vitro . Above this temperature, we can also observe in vivo aggregation that results in the complete disappearance of the enzyme from the soluble fraction. Moreover, reducing the in vivo level of HTS aggregation enables growth at non‐permissive temperatures. This is the first demonstration of the physiological role of aggregation of a specific protein in the growth of wild‐type bacteria.