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In vivo protein folding: suppressor analysis of mutations in the groES cochaperone gene of Escherichia coli
Author(s) -
ZeilstraRyalls Jill,
Fayet Olivier,
Georgopoulos Costa
Publication year - 1996
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.10.1.8566535
Subject(s) - groel , groes , chaperone (clinical) , biology , escherichia coli , mutant , genetics , gene , protein folding , microbiology and biotechnology , medicine , pathology
Our previous work has shown that the Escherichia coli groES14 and groES15 mutations result in reduced GroE chaperone machine function. By selecting for restoration of the ability of those mutant groES alleles to suppress the thermosensitivity of bacteria bearing the dnaA46 mutation, we isolated a number of intra‐ and extragenic suppressors that increase in vivo GroE chaperone function. One of the intragenic suppressors has been mapped to a segment that codes for the GroES mobile loop, previously shown to be indispensable for proper GroES/GroEL interaction. Two extragenic suppressors have been mapped to a groEL segment, previously identified by mutational analysis as coding for an important functional region of the GroEL protein. Our results should contribute to our eventual understanding of the structure‐function relationships of the universally conserved GroE chaperone machine.—Zeilstra‐Ryalls, J., Fayet, O., Georgopoulos, C. In vivo protein folding: suppressor analysis of mutations in the groES cochaperone gene of Escherichia coU. FASEB J. 10, 148‐152 (1996)