Evidence that the two Escherichia coli groE morphogenetic gene products interact in vivo

Tilly, Kit; Georgopoulos, Costa

doi:10.1128/jb.149.3.1082-1088.1982

Cited by 83 publications

(23 citation statements)

References 16 publications

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“…The two mutants carrying groES619 or groEL44 were compared with wild-type strain. These mutants exhibit temperature-sensitive cell growth and do not support growth of bacteriophage X (Georgopoulos and Eisen, 1974;Tilly and Georgopoulos, 1982). Each strain was transformed with pBR322 or its derivative to allow the expression of Bla from the plasmid-encoded bla gene.…”

Section: Resultsmentioning

confidence: 99%

Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.

et al. 1989

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Escherichia coli heat‐shock proteins GroES and GroEL are essential cytoplasmic proteins, which have been termed ‘chaperonins’ because of their ability to assist protein assembly of bacteriophage capsids and multimeric enzymes of foreign origin. In this report we show that temperature‐sensitive mutations in groES and groEL genes cause defective export of the plasmid‐encoded beta‐lactamase (Bla) in vivo. Since efficient translocation of proteins across biological membranes is thought to be supported by cytoplasmic factors that protect presecretory molecules from being misfolded, these results suggest that both GroES and GroEL proteins possess a chaperone function by which they facilitate export of Bla. The translocation of other secretory proteins, however, appears to depend minimally on GroE, suggesting that GroE interacts only with a specific class of secreted proteins.

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Section: Resultsmentioning

confidence: 99%

Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.

et al. 1989

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“…The molecular details of this protection are not yet fully understood, but recent work indicates that the biological function of CA is to facilitate assembly and folding of protein subunits within the cytoplasm [8,11,12]. Genetic and experimental evidence suggest that the function of the E. coli GroEL is dependent on the interaction with another protein, the GroES 15 kDa protein [13]. The experimental evidence implicating CA in the pathogenesis of autoimmune disease [7,[14][15][16][17][18] makes it important to obtain comparative sequence data for several CAs.…”

Section: Introductionmentioning

confidence: 99%

Sequence analysis of the Legionella micdadei groELS operon

Hindersson

1991

FEMS Microbiology Letters

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A 2.7 kb DNA fragment encoding the 60 kDa common antigen (CA) and a 13 kDa protein of Legionella micdadei was sequenced. Two open reading frames of 57,677 and 10,456 Da were identified, corresponding to the heat shock proteins GroEL and GroES, respectively. Typical -35, -10, and Shine-Dalgarno heat shock expression signals were identified upstream of the L. micdadei groEL gene. Further upstream, a poly-T region, also a feature of the sigma 32-regulated Escherichia coli groELS heat shock operon, was found. Despite the high degree of homology of the expression signals in E. coli and L. micdadei, Western blot analysis with an L. micdadei specific anti-groEL antibody did not reveal a significant increase in the amount of the GroEL protein during heat shock in L. micdadei or in the recombinant E. coli expressing L. micdadei GroEL.

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“…The two E. coli mutants carrying groES619 (NRK233) and groEL44 (NRK117) were used. These mutants exhibit temperature-sensitive cell growth and do not support the growth of bacteriophage X (14,29). Each strain was transformed with pSYW122 (carrying whole V cholerae groESL), pSYW125 (carrying V cholerae groES), pSYW128 (carrying V cholerae groEL) or pUC 19, and complementation of the temperature-sensitive growth phenotype of the mutants was examined (Fig.…”

Section: Rescue Ofe Coli Groe Mutants With V Cholerae Groesl Genesmentioning

confidence: 99%

Cloning, Sequencing, and Functional Expression in Escherichia coli of Chaperonin (groESL) Genes from Vibrio cholerae

Mizunoe

Wai

Umene

et al. 1999

Microbiology and Immunology

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Using a series of oligonucleotides synthesized on the basis of conserved nucleotide motifs in heatshock genes, the groESL heat-shock operon from a Vibrio cholerae TSI-4 strain has been cloned and sequenced, revealing that the presence of two open reading frames (ORFs) of 291 nucleotides and 1,632 nucleotides separated by 54 nucleotides. The first ORF encoded a polypeptide of 97 amino acids, GroES homologue, and the second ORF encoded a polypeptide of 544 amino acids, GroEL homologue. A comparison of the deduced amino acid sequences revealed that the primary structures of the V. cholerae GroES and GroEL proteins showed significant homology with those of the GroES and GroEL proteins of other bacteria. Complementation experiments were performed using Escherichia coli groE mutants which have the temperature-sensitive growth phenotype. The results showed that the groES and groEL from V. cholerae were expressed in E. coli, and groE mutants harboring V. cholerae groESL genes regained growth ability at high temperature. The evolutionary analysis indicates a closer relationship between V. cholerae chaperonins and those of the Haemophilus and Yersinia species.

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Evidence that the two Escherichia coli groE morphogenetic gene products interact in vivo

Cited by 83 publications

References 16 publications

Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.

Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.

Sequence analysis of the Legionella micdadei groELS operon

Cloning, Sequencing, and Functional Expression in Escherichia coli of Chaperonin (groESL) Genes from Vibrio cholerae

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