Posttranslational modification and processing of membrane lipoproteins in bacteria

Wu, Henry C.; Tokunaga, Masao; Tokunaga, Hiroko; Hayashi, Shigeru; Giam, Chou-Zen

doi:10.1002/jcb.240220305

Cited by 58 publications

(64 citation statements)

References 39 publications

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“…Heavy and light shading indicates positions at which at least six of the seven are identical or similar respectively. The solid arrow indicates the site at which the lipoprotein leader sequence is predicted to be cleaved during modification by signal peptidase II (Wu et al, 1983). The absence of a negatively charged residue following the cysteine at this site would predict that Pcp Sm and Pcp Ec are localized to the outer membrane (Yamaguchi et al, 1988), as has been found for the other lipoproteins shown.…”

Section: Identification Of Rapmentioning

confidence: 90%

“…The second of the complete ORFs, orf3 (468 bp) was predicted to encode a 15 540 Da protein of 155 amino acids. The first 17 amino acids of this protein were characteristic of an N-terminal sec-dependent signal sequence, with a recognition sequence (LVGC) for lipid modification and processing by signal peptidase II (Wu et al, 1983;Yamaguchi et al, 1988). Consistent with this, the predicted protein product shared a high level of sequence identity with Pcp Ye (71%), Pcp Hi (47%) and SlyB (71%), all of which have been classified previously as outer membrane lipoproteins from Yersinia enterocolitica, Haemophilus influenzae and Salmonella typhimurium respectively (Deich et al, 1988;Baumler and Hantke, 1992;Ludwig et al, 1995;Fig.…”

Section: Subcloning and Sequencingmentioning

confidence: 99%

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The Rap and Hor proteins of Erwinia, Serratia and Yersinia: a novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens

Thomson

Cox

Bycroft

et al. 1997

Molecular Microbiology

109

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SummaryThe enteric bacterium Serratia marcescens is an opportunistic human pathogen. The strain ATCC39006 makes the red pigment, prodigiosin (Pig), and the ␤-lactam antibiotic carbapenem (Car). Mutants were isolated that were concomitantly defective for Pig and Car production. These mutants were found to have a mutation in the rap gene (regulation of antibiotic and pigment). Sequence analysis of the rap gene revealed a predicted protein product showing strong homology to SlyA, originally thought to be a haemolytic virulence determinant in Salmonella typhimurium. Homologues of rap were detected in several bacterial genera, including Salmonella, Yersinia, Enterobacter, and species of the plant pathogen, Erwinia. The Erwinia hor Er (homologue of rap) and the Yersinia hor Ye genes were also found to be very similar to rap and slyA. Marker exchange mutagenesis of hor Er revealed that it encoded a regulatory protein controlling the production of antibiotic and exoenzyme virulence determinants in the phytopathogen, Erwinia carotovora subspecies carotovora. We have shown that these new homologues of SlyA form a highly conserved subgroup of a growing superfamily of bacterial regulatory proteins controlling diverse physiological processes in human, animal and plant pathogens.

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Section: Identification Of Rapmentioning

confidence: 90%

Section: Subcloning and Sequencingmentioning

confidence: 99%

The Rap and Hor proteins of Erwinia, Serratia and Yersinia: a novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens

Thomson

Cox

Bycroft

et al. 1997

Molecular Microbiology

109

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“…They all contain a signal peptide with a sequence at the cleavage site resembling the consensus lipoprotein modification sequence described by Wu et al (38). The polypeptide chain of the mature form is small: 33 amino acids for the colicin A lysis (Cal) protein and 28 amino acids for colicin El, E2, and E3 and cloacin DF13 lysis proteins.The consensus sequence for lipoproteins, Leu-Ala-GlyCys (12,20,38), constitutes the recognition site for lipid modification enzymes. A glyceride thioether is formed on the cysteine residue, after which lipoprotein is processed by signal peptidase II between the glycine and cysteine residues.…”

mentioning

confidence: 99%

“…The consensus sequence for lipoproteins, Leu-Ala-GlyCys (12,20,38), constitutes the recognition site for lipid modification enzymes. A glyceride thioether is formed on the cysteine residue, after which lipoprotein is processed by signal peptidase II between the glycine and cysteine residues.…”

mentioning

confidence: 99%

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Lipoprotein nature of the colicin A lysis protein: effect of amino acid substitutions at the site of modification and processing

Cavard¹,

Baty²,

Howard³

et al. 1987

J Bacteriol

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The colicin A lysis protein (Cal) is required for the release of colicin A to the medium by producing bacteria. This protein is produced in a precursor form that contains a cysteine at the cleavage site (-Leu-Ala-Ala-Cys). The precursor must be modified by the addition of lipid before it can be processed. The maturation is prevented by globomycin, an inhibitor of signal peptidase II. Using oligonucleotide-directed mutagenesis, the alanine and cysteine residues in the -1 and + 1 positions of the cleavage site were replaced by proline and threonine residues, respectively, in two different constructs. Both substitutions prevented the normal modification and cleavage of the protein. The marked activation of the outer membrane detergent-resistant phospholipase A observed with wild-type Cal was not observed with the Cal mutants. Both Cal mutants were also defective for the secretion of colicin A. In one mutant, the signal peptide appeared to be cleaved off by an alternative pathway involving signal peptidase I. Electron microscope studies with immunogold labeling of colicin A on cryosections of pidA and cal mutant cells indicated that the colicin remains in the cytoplasm and is not transferred to the periplasmic space. These results demonstrate that Cal must be modified and processed to activate the detergent-resistant phospholipase A and to promote release of colicin A.Proteins of low molecular weight called lysis protein are required for the release of colicins or cloacin from Escherichia coli producing cells (7,13,21,31,33). The genes that encode these proteins are located downstream of the immunity genes on the colicin plasmid. They are organized in operons with the corresponding colicin structural genes (8,13,23,34). Their expression is thus under the same regulation as that of the colicin structural genes, but they seem to be produced in lower amounts than the colicins owing to the presence of a transcription terminator after the colicin structural gene (10,13,26).The structures of the five known lysis proteins feature a high degree of homology (7,8,13,35). They all contain a signal peptide with a sequence at the cleavage site resembling the consensus lipoprotein modification sequence described by Wu et al. (38). The polypeptide chain of the mature form is small: 33 amino acids for the colicin A lysis (Cal) protein and 28 amino acids for colicin El, E2, and E3 and cloacin DF13 lysis proteins.The consensus sequence for lipoproteins, Leu-Ala-GlyCys (12,20,38), constitutes the recognition site for lipid modification enzymes. A glyceride thioether is formed on the cysteine residue, after which lipoprotein is processed by signal peptidase II between the glycine and cysteine residues. This signal peptidase is specifically inhibited by globomycin, a cyclic peptide antibiotic (15, 35). After processing, a fatty acid is covalently attached to the N-terminal cysteine.The Cal protein, encoded by the cal gene, has the sequence Leu-Ala-Ala-Cys at the end of its signal sequence, that is, the lipoprotein consensus sequence in ...

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What Can We Learn from Colicins about the Dynamics of Insertion and Transfer of Proteins into and Across Membranes

Lazdunski¹

1988

Membrane Biogenesis

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Posttranslational modification and processing of membrane lipoproteins in bacteria

Cited by 58 publications

References 39 publications

The Rap and Hor proteins of Erwinia, Serratia and Yersinia: a novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens

The Rap and Hor proteins of Erwinia, Serratia and Yersinia: a novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens

Lipoprotein nature of the colicin A lysis protein: effect of amino acid substitutions at the site of modification and processing

What Can We Learn from Colicins about the Dynamics of Insertion and Transfer of Proteins into and Across Membranes

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