Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene

Conlin, C A; Trun, Nancy; Silhavy, Thomas J.; Miller, Charles G.

doi:10.1128/jb.174.18.5881-5887.1992

Cited by 37 publications

(18 citation statements)

References 18 publications

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“…Interestingly, independent of its effect on natural signal peptides, OpdA was also identified in suppressor screens using secretory proteins with defective signal peptides. In such screens, it was noticed that the prlC (protein localization) mutation, which turned out to be a mutation in the opdA gene, could suppress the export defect of certain LamB signal sequence mutants (57). At present, it is not clear how mutations in OpdA can lead to the observed prlC phenotype.…”

Section: Sppasesmentioning

confidence: 99%

Signal Peptide-Dependent Protein Transport in Bacillus subtilis : a Genome-Based Survey of the Secretome

Tjalsma

Bolhuis

Jongbloed

et al. 2000

Microbiol Mol Biol Rev

751

768

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SUMMARY One of the most salient features of Bacillus subtilis and related bacilli is their natural capacity to secrete a variety of proteins into their environment, frequently to high concentrations. This has led to the commercial exploitation of bacilli as major “cell factories” for secreted enzymes. The recent sequencing of the genome of B. subtilis has provided major new impulse for analysis of the molecular mechanisms underlying protein secretion by this organism. Most importantly, the genome sequence has allowed predictions about the composition of the secretome, which includes both the pathways for protein transport and the secreted proteins. The present survey of the secretome describes four distinct pathways for protein export from the cytoplasm and approximately 300 proteins with the potential to be exported. By far the largest number of exported proteins are predicted to follow the major “Sec” pathway for protein secretion. In contrast, the twin-arginine translocation “Tat” pathway, a type IV prepilin-like export pathway for competence development, and ATP-binding cassette transporters can be regarded as “special-purpose” pathways, through which only a few proteins are transported. The properties of distinct classes of amino-terminal signal peptides, directing proteins into the various protein transport pathways, as well as the major components of each pathway are discussed. The predictions and comparisons in this review pinpoint important differences as well as similarities between protein transport systems in B. subtilis and other well-studied organisms, such as Escherichia coli and the yeast Saccharomyces cerevisiae. Thus, they may serve as a lead for future research and applications.

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Section: Sppasesmentioning

confidence: 99%

Signal Peptide-Dependent Protein Transport in Bacillus subtilis : a Genome-Based Survey of the Secretome

Tjalsma

Bolhuis

Jongbloed

et al. 2000

Microbiol Mol Biol Rev

751

768

View full text Add to dashboard Cite

show abstract

“…The amino acid sequence shows strong similarity to another bacterial peptidase (dipeptidyl carboxypeptidase, encoded by dcp) and to a mammalian metalloprotease (rat metallopeptidase EP 24.15) that is involved in the processing of peptide hormones (9). Evidence presented in the accompanying article shows that opdA4 is the Salmonella homolog of the E. coliprlC gene (10).…”

mentioning

confidence: 93%

“…Other thiolutin resistance mutations have been mapped to 11 and 85 map units in E. coli (36). opdA maps at 76 map units on the S. typhimurium chromosome (9), and priC, the E. coli homolog of opdA (10), maps at 71 map units on the E. coli chromosome (39). Although the relationship between the thiolutin resistance mutations and opd4 is unknown, the map positions of the E. coli mutations suggest that they affect different genes.…”

Section: Methodsmentioning

confidence: 99%

Oligopeptidase A is required for normal phage P22 development

1992

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The opdA gene of SalmoneUla typhimurium encodes an endoprotease, oligopeptidase A (OpdA). Strains carying opd4 mutations were deficient as hosts for phage P22. P22 and the closely related phages L and A3 formed tiny plaques on an opdA host. SalmoneUla phages 9NA, KB1, and ES18.hl were not affected by opdA mutations. Although opd4 strains displayed normal doubling times and were infected by P22 as efficiently as opdA+ strains, the burst size of infectious particles from an opd4 host was less than 1/10 of that from an opdA + host. This decrease resulted from a reduced efficiency of plating of particles from an opdAl infection. In the absence of a functional opdA4 gene, most ofthe P22 particles are defective. To identify the target of OpdA action, P22 mutants which formed plaques larger than wild-type plaques on an opdA mutant lawn were isolated.Marker rescue experiments using cloned fragments of P22 DNA localized these mutations to a 1-kb fragment.The nucleotide sequence of this fragment and a contiguous region (including all of both P22 gene 7 and gene 14) was determined. The mutations leading to opdA independence affected the region of gene 7 coding for the amino terminus of gp7, a protein required for DNA injection by the phage. Comparison of the nucleotide sequence with the N-terminal amino acid sequence of gp7 suggested that a 20-amino-acid peptide is removed from gp7 during phage development. Further experiments showed that this processing was opd4 dependent and rapid (half-life, <2 min) and occurred in the absence of other phage proteins. The opd4-independent mutations lead to mutant forms of gp7 which function without processing.Oligopeptidase A (OpdA) was identified by Vimr and Miller (42) as one of two enzymes in extracts of Salmonella typhimurium which hydrolyzed N-acetyl-L-Ala4. OpdA has been purified from both Escherichia coli (28) and S. typhimurium (9). Novak et al. (28) and Novak and Dev (27) have shown that OpdA is a signal peptide peptidase. In vitro, OpdA is the major soluble enzyme able to hydrolyze the E. coli lipoprotein signal peptide. Substrate specificity studies indicate that OpdA is an endopeptidase with a preference for Ala and Gly residues (27,28,41). Its inhibition by metal chelators (9, 28) suggests that it is a metallopeptidase.The gene encoding OpdA, opdA, has been cloned and sequenced (9). The predicted amino acid sequence of the 77-kDa OpdA protein contains a thermolysin-type metalloprotease Zn2+-binding site (9,22). The amino acid sequence shows strong similarity to another bacterial peptidase (dipeptidyl carboxypeptidase, encoded by dcp) and to a mammalian metalloprotease (rat metallopeptidase EP 24.15) that is involved in the processing of peptide hormones (9). Evidence presented in the accompanying article shows that opdA4 is the Salmonella homolog of the E. coliprlC gene (10).Mutant alleles of prlC suppress the localization defect of certain signal peptide mutations (39).Mutations in opdA were originally isolated by screening for mutants unable to use AcAla4 as a sole nitro...

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“…We have shown that prlC is the Escherichia coli homolog of the Salmonella typhimurium gene opdA, which encodes metallopeptidase oligopeptidase A (4). We have sequenced both of these genes and shown that their nucleotide sequences are 84% identical (4). Sequence comparisons with other proteases have shown that OpdA and PrlC are members of a class of metallopeptidases which includes enzymes from rats, pigs, Schizophyllum commune, and Saccharomyces cerevisiae.…”

mentioning

confidence: 99%