A mutation in the gene for trigger factor suppresses the defect in cell division in the divE42 mutant of Escherichia coli K12

Molecular and General Genetics

Volumn 260, Issue 1, 1998, Pages 75-80

  Nakano, H ^a   Yamada, Y ^b   Ishikura, H ^b   Inokuchi, H ^a  

^a KYOTO UNIVERSITY   (Japan)

^b JICHI MEDICAL UNIVERSITY   (Japan)

Author keywords

Cold sensitivity; divE42 mutant; serT; Trigger factor

Indexed keywords

ISOMERASE;

ARTICLE; BACTERIUM MUTANT; CELL DIVISION; CLONE; COLD SENSITIVITY; DNA SEQUENCE; ESCHERICHIA COLI K 12; GENE LIBRARY; GENE MUTATION; PHENOTYPE; PRIORITY JOURNAL; SUPPRESSOR GENE;

BETA-GALACTOSIDASE; CELL DIVISION; ESCHERICHIA COLI; GENE EXPRESSION; GENES, BACTERIAL; GENETIC COMPLEMENTATION TEST; MODELS, GENETIC; MUTATION; PEPTIDYLPROLYL ISOMERASE; RNA, TRANSFER, SER; SEQUENCE ANALYSIS, DNA; SEQUENCE DELETION; SUPPRESSION, GENETIC; TEMPERATURE;

EID: 0031786840     PISSN: 00268925     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004380050872     Document Type: Article

References (17)

1. Callebaut I, Mornon JP (1995) Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family. FEBS Lett 374:211-215
2. Guthrie B, Wickner W (1990) Trigger factor depletion or over-production causes defective cell division but does not block protein export. J Bacteriol 172:5555-5562
3. Hesterkamp T, Bukau B (1996) Identification of the prolyl isomerase domain of Escherichia coli trigger factor. FEBS Lett 385:67-71
4. Hesterkamp T, Deuerling E, Bukau B (1997) The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. J Biol Chem 272: 21865-21871
5. Kandor O, Sherman M, Rhode M, Goldberg AL (1995) Trigger factor is involved GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. EMBO J 14:6021-6027
6. Kohara Y, Akiyama K, Isono K (1987) The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50:495-508
7. Miller JH (1972) Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
8. Norrander J, Kempe T, Messing J (1983) Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis. Gene 26:101-106
9. Ohki M (1972) Correlation between metabolism of phosphatidylglycerol and membrane synthesis in Escherichia coli. J Mol Biol 68: 249-264
10. Ohki M, Mitsui H (1974) Defective membrane synthesis in an E. coli mutant. Nature 252:64-66
11. Ser). Cell Sci 8:704-713
12. Sambrook J, Fritsch EF, Maniatis T (1989) Molecular Cloning. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
13. Stoller G, Rücknagel KP, Nierhaus KH, Schmid FX, Fischer G, Rahfeld JU (1995) A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J 14:4939-4948
14. Stoller G, Tradler T, Rücknagel KP, Rahferld JU, Fischer G (1996) An 11.8 kDa proteolytic fragment of E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity. FEBS Lett 384:117-122
15. Ser. EMBO J 3:1103-1107
16. Ser genes. Nucleic Acids Res 22:3124-3130
17. Yamaguchi K, Masamune Y (1985) Autogenous regulation of synthesis of the replication protein in plasmid pSC101. Mol Gen Genet 200:362-367