In vivo protein folding: suppressor analysis of mutations in the groES cochaperone gene of Escherichia coli.
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
J
Department of Microbiology and Molecular Genetics, University of Texas Health Science Center at Houston 77225, USA.
Fayet
O
O
Georgopoulos
C
C
D001426:Bacterial Proteins / Q000235:genetics; D010582:Bacteriophage lambda / Q000254:growth & development; D018835:Chaperonin 10 / Q000235:genetics; D018834:Chaperonin 60 / Q000235:genetics; D018833:Chaperonins / Q000235:genetics*; D002874:Chromosome Mapping; D004268:DNA-Binding Proteins / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D006360:Heat-Shock Proteins / Q000235:genetics; D006358:Hot Temperature; D016296:Mutagenesis; D010957:Plasmids / Q000235:genetics; D017510:Protein Folding; D017422:Sequence Analysis, DNA; D013489:Suppression, Genetic
D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D004268:DNA-Binding Proteins; C066312:DnaA protein, Bacteria; D029968:Escherichia coli Proteins; C028715:GroE protein, E coli; D006360:Heat-Shock Proteins; D018833:Chaperonins