Affiliation:
1. Department of Molecular Biology, Umeå University, S-90187 Umeå, Sweden
Abstract
ABSTRACT
We have found that the cyclic AMP (cAMP) receptor protein (CRP)-cAMP regulatory complex in
Escherichia coli
is subject to osmoregulation at the level of
crp
gene expression. This osmoregulation was lost in a
cya
mutant strain but could be restored by external addition of cAMP, suggesting that the intracellular level of cAMP is a key factor in the osmoregulation of CRP. The ability of the cell to maintain optimal CRP activity was essential for the growth and survival of the bacteria under low-osmolarity conditions as shown by studies with different
crp
mutant alleles. A suppressor mutant with a novel amino acid substitution (L124R) in CRP showed restored growth at low osmolarity. CRP(L124R) was not activated by cAMP and was shown to be dominant negative over the wild type. Our findings suggest that the fine-tuning of the CRP activity may be critical for bacterial viability and adaptability to changing osmotic conditions.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
45 articles.
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