The major outer membrane lipoprotein and new lipoproteins share a common signal peptidase that exists in the cytoplasmic membrane of <i>Escherichia coli</i>

Yamada, H.; Yamagata, Hideo; Mizushima, Shôji

doi:10.1016/0014-5793(84)80068-x

Cited by 30 publications

(9 citation statements)

References 14 publications

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“…{Lanes 1,5,9) BZR60 pGP1-2 pDMS9; (lanes 2,6,10) DK2179 pGP1-2 pDMS9; (lanes 3,7,11) BZR60 pGP1-2 pRIN2A.7; (lanes 4, 8, 12) DK2179 pGP1-2 pRIN2A.7. (Yamada et al 1984) with globomycin treatment also did not alter TcpA processing. Thus, it appears that TcpJ functions independently to specifically cleave the leader peptide from precursor TcpA.…”

Section: Discussionmentioning

confidence: 85%

“…TcpA processing m the presence of globomycin E. coli encodes a second leader peptidase for processing of glyceride-modified lipoprotein precursors (Yamada et al 1984). To exclude use of lipoprotein-specific leader peptidase in TcpA processing, a T7 assay was performed in the presence of the antibiotic globomycin, a potent inhibitor of the lipoprotein peptidase (Hussain et al 1980).…”

Section: Tcpa Processing In a Leader Peptidase Mutantmentioning

confidence: 99%

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Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.

Kaufman¹,

Seyer²,

Taylor³

1991

Genes Dev.

103

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Biogenesis of the Vibrio cholerae toxin-coregulated pilus (TCP) requires the activities of at least seven accessory proteins. We demonstrate that a portion of this pathway involves a novel processing step in which a hydrophilic leader peptide is proteolytically removed from TcpA by the gene product characterized in this report, TcpJ, to yield the mature, export-competent form of the pilin. Cleavage of the pilin leader peptide is independent of known signal peptidases as demonstrated by pilin-processing profiles in Escherichia coli strains conditionally defective for production of leader peptidase or grown in the presence of the antibiotic globomycin. Additionally, pilin cleavage did not rely on the SecA protein, as evidenced by TcpA processing in azide-treated cells. These results suggest that TcpJ is representative of a new class of proteins involved in SecA-independent proteolytic cleavage of a set of atypical leader peptides during extracellular export.

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Section: Discussionmentioning

confidence: 85%

Section: Tcpa Processing In a Leader Peptidase Mutantmentioning

confidence: 99%

Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.

Kaufman¹,

Seyer²,

Taylor³

1991

Genes Dev.

103

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“…SPase I is responsible for the processing of the precursor of bacteriophage M13 coat protein and the majority of exported pre-proteins (Dalbey & Wickner, 1985;Wolfe et al, 1982). SPase I1 exclusively processes glyceride-modified lipoproteins (Tokunaga et al, 1982 ;Yamada et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

Non-functional expression of Escherichia coli signal peptidase I in Bacillus subtilis

Dijl¹,

Jong²,

Smith³

et al. 1991

Journal of General Microbiology

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The Escherichia cofi fep gene, encoding signal peptidase I (SPase I) was provided with Baciffus subtifis transcription/translation signals and expressed in this organism. When present on a low-copy-number plasmid, the amount of E. cofi SPase I produced (per mg cell protein) in B. subtifis was half that produced in wild-type E. cofi cells. The production of E. cofi SPase I in B. subtifis was increased approximately fivefold by cloning the fep gene into a high-copy-number plasmid. The expression of E cofi SPase I in B. subtifis did not appear to increase the rate of processing of two hybrid secretory precursor proteins. Two observations may explain the failure of E. cofi SPase I to stimulate processing of exported proteins in B. subtifis. First, the E. cofiSPase I was apparently not exposed on the outside of the B. subtifis cytoplasmic membrane, indicating its incorrect insertion into the membrane. Second, in vi?ro processing studies, using cell-free extracts of B. subtilis producing E. cofi SPase I, suggested that the enzyme was not active. A further outcome of this study was that conditions favouring processing of precursors by SPase I in cell-free extracts of E. cofi did not favour processing by the corresponding enzyme in B. subtifis cell-free extracts. This suggests that significant differences exist between the two enzymes. The observation that antibodies directed against E. cofi SPase I did not cross-react with B. subtifis membrane proteins supports this idea.

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“…In E. coli they are processed by a specific lipoprotein signal peptidase (30,33), and bacilli appear to have enzymes with similar specificity (16). The prelipoproteins show a conserved sequence, LeuAla-Gly-Cys, around the site of lipid modification and processing (24,32).…”

mentioning

confidence: 99%

“…Therefore, we have assumed that Cys-+ 1 undergoes lipid modification, although Cys--6 may also be modified to some extent (8). Presumably the processing site for lipoprotein signal peptidase (Lsp [30,33]) is between Gly-1 and Cys-+1. The calculated molecular size of the resulting protein (287 amino acid residues with Cys-+1 as the NH2 terminus) is 31,740 daltons.…”

mentioning

confidence: 99%

Cloning and sequencing of the blaZ gene encoding beta-lactamase III, a lipoprotein of Bacillus cereus 569/H

Hussain¹,

Pastor²,

Lampen³

1987

J Bacteriol

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It has not been clear whether the membrane-bound Il-lactamase III of Bacillus cereus 569 is a separate enzyme or a modified form of the secreted Il-lactamase I. The membrane enzyme is an acyl-glyceride thioether-linked lipoprotein (J. B. K. Nielsen and J. Q. Lampen, Biochemistry 22:4652-4656, 1983) and thus is probably a separate entity. We cloned the P-lactamase III gene (blaZ) on a 4.9-kilobase-pair ClaI fragment from mutant strain 569/H (constitutive for high-level production of 3-lactamases I, II, and III), and the nucleotide sequence was determined. The structural gene was flanked by typical promoter, transcription termination, and translation initiation sequences. Expression of the cloned gene in Escherichia coli was low in exponential-phase cultures and increased only as the cultures reached the stationary phase. The deduced amino acid sequence indicates a pre-p-lactamase III of 316 amino acid residues (35,021 daltons), with a 29-residue signal peptide and a mature lipoprotein form of -32,500 daltons. The 12 NH2-terminal residues of a 21-kilodalton tryptic peptide from the B. cereus membrane enzyme were in agreement with the sequence deduced from the cloned gene. The amino acid sequence was highly homologous to the class A P-lactamases, especially that of Bacillus licheniformis 749, f-Lactamase III is a distinct class A enzyme and the product of a separate gene (blaZ).Bacillus cereus 569/H is unusual in that it makes three different P-lactamases.

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The major outer membrane lipoprotein and new lipoproteins share a common signal peptidase that exists in the cytoplasmic membrane of Escherichia coli

Cited by 30 publications

References 14 publications

Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.

Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.

Non-functional expression of Escherichia coli signal peptidase I in Bacillus subtilis

Cloning and sequencing of the blaZ gene encoding beta-lactamase III, a lipoprotein of Bacillus cereus 569/H

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