groE mutants of Escherichia coli are defective in umuDC-dependent UV mutagenesis.
Overexpression of the SOS-inducible umuDC operon of Escherichia coli results in the inability of these cells to grow at 30 degrees C. Mutations in several heat shock genes suppress this cold sensitivity. Suppression of umuD+C+-dependent cold sensitivity appears to occur by two different mechanisms. We show that mutations in lon and dnaK heat shock genes suppress cold sensitivity in a lexA-dependent manner. In contrast, mutations in groES, groEL, and rpoH heat shock genes suppress cold sensitivity regardless of the transcriptional regulation of the umuDC genes. We have also found that mutations in groES and groEL genes are defective in umuDC-dependent UV mutagenesis. This defect can be suppressed by increased expression of the umuDC operon. The mechanism by which groE mutations affect umuDC gene product function may be related to the stability of the UmuC protein, since the half-life of this protein is shortened because of mutations at the groE locus.
Donnelly
C E
CE
Biology Department, Massachusetts Institute of Technology, Cambridge 02139.
Walker
G C
GC
D000942:Antigens, Bacterial / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics*; D018835:Chaperonin 10; D018834:Chaperonin 60; D004259:DNA-Directed DNA Polymerase; D004926:Escherichia coli / Q000235:genetics* / Q000254:growth & development / Q000528:radiation effects; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D005838:Genotype; D006360:Heat-Shock Proteins / Q000235:genetics*; D009154:Mutation; D009876:Operon; D010957:Plasmids; D013014:SOS Response, Genetics; D013696:Temperature; D014466:Ultraviolet Rays
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D004259:DNA-Directed DNA Polymerase; C055218:UmuD protein, E coli