Cited by 71Bacterial Genetics and BiotechnologyLipid Membrane Structure and BehaviorBiochemical and Structural Characterization

Glyceride-cysteine lipoproteins and secretion by Gram-positive bacteria

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Nielsen, J B, Lampen, J O·1982·Journal of Bacteriology

Abstract

The membrane penicillinases of Bacillus licheniformis and Bacillus cereus are lipoproteins with N-terminal glyceride thioether modification identical to that of the Escherichia coli outer membrane lipoprotein. They are readily labeled with [3H]palmitate present during exponential growth. At the same time, a few other proteins in each organism become labeled and can be detected by fluorography after sodium dodecyl sulfate-polyacrylamide gel electrophoresis of total membrane proteins. We distinguish these proteins from the O-acyl proteolipids by demonstrating the formation of glyceryl cysteine sulfone after performic acid oxidation and hydrolysis of the protein. By this criterion, B. licheniformis and B. cereus contain sets of lipoproteins larger in average molecular weight than that of E. coli. Members of the sets probably are under a variety of physiological controls, as indicated by widely differing relative labeling intensity in different media. The set in B. licheniformis shares with membrane penicillinase a sensitivity to release from protoplasts by mild trypsin treatment, which suggests similar orientation on the outside of the membrane. At least one protein is the membrane-bound partner of an extracellular hydrophilic protein, the pair being related as membrane and exopenicillinases are. We propose that the lipoproteins of gram-positive organisms are the functional equivalent of periplasmic proteins in E. coli and other gram-negative bacteria, prevented from release by anchorage to the membrane rather than by a selectively impermeable outer membrane.

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Crossref · 10.1128/jb.152.1.315-322.1982

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  • Insertion of proteins into the plasma membrane via an N-terminal diacyl-glycerol modification occurs for BlaZ of Staphylococcus aureus.

    “(v) Insertion of proteins into the plasma membrane via an N-terminal diacyl-glycerol modification (BlaZ of Staphylococcus aureus) [12,13].”

    From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [12]

    The Discussion (page not available) identifies the membrane-bound penicillinase of S. aureus as a glyceride-cysteine lipoprotein, supporting the membrane-anchoring mechanism attributed to the source. The copy describes an acyl-glyceride modification but does not establish the more specific diacyl-glycerol structure for the S. aureus protein. (LLM, conf=0.82)

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  1. Haegoua S. and M. Inouye. 1980. Biosynthesis and assembly of the outer membrane proteins p. 67-114. M. Inouye (ed.) In Bacterial outer membranes. Wiley Interscience New York.

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Authors
Nielsen, J. B., & Lampen, J. O.
Venue
Journal of Bacteriology
Published
1982-10
Volume
152
Issue
1
Pages
315-322
ISSN
  • 0021-9193 (ISSN-L)
  • 1098-5530
OpenAlex
W1518677115
Cited by
71
References
30
Citations by year
2025: 1 · 2020: 1 · 2017: 1 · 2016: 1 · 2014: 5 · 2013: 1 · 2012: 1
FWCI
2.93
Type
journal article
Language
en
Open access
Locations
  • Journal of Bacteriology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords
Bacillus licheniformis, Bacillus cereus, exoproteins, membrane protein secretion, periplasmic proteins, trypsin sensitivity, protoplasts, Gram-positive bacteria
MeSH terms
Bacillus, Bacillus cereus, Bacterial Proteins, Chemistry, Cysteine, Hydrolysis, Lipoproteins, Membrane Proteins, Penicillinase, Sulfones, Chemical Phenomena

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