Palmitoylation of membrane proteins inSpiroplasma floricola

Borovsky, Zipora; Sinnreich, Michael; Rottem, Shlomo

doi:10.1007/bf01570900

Current Microbiology

1992

DOI: 10.1007/bf01570900

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Palmitoylation of membrane proteins inSpiroplasma floricola

Zipora Borovsky

Michael Sinnreich

Shlomo Rottem

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Cited by 4 publications

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“…Previous studies with S. melliferum spiralin, antigenically related to S. citri spiralin (40), have shown that spiralin is a lipoprotein (37). As frequently observed for mollicute membrane proteins (2,10,11,28), S. melliferum spiralin becomes preferentially labeled with palmitic acid when radioactive fatty acids are present in the culture medium.Comparison of the spiralin genes of S. citri and S. melliferum has shown that the two genes have a conserved N-terminal end. In the latter study, the strain of S. citri used was R8A2HP.…”

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Spiralin polymorphism in strains of Spiroplasma citri is not due to differences in posttranslational palmitoylation

et al. 1996

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Spiralin is defined as the major membrane protein of the helical mollicute Spiroplasma citri. According to the S. citri strain used, spiralin shows polymorphism in its electrophoretic mobility. The spiralin gene sequences of eight S. citri strains were determined by direct sequencing of the PCR-amplified genes. All spiralins were found to be 241 amino acids long, except for the spiralin of strain Palmyre, which is 242 amino acids long. The molecular masses calculated from these sequences did not explain the differences observed in the electrophoretic mobilities. In all of the spiralins examined, the first 24 N-terminal amino acids were conserved, including a cysteine at position 24, and had the features of typical signal peptides of procaryotic lipoproteins. When S. citri strains were grown in the presence of [ ]palmitic acid labeled, and it had almost the same electrophoretic mobility irrespective of the spiralins used. Samples of the unlabeled peptide fragments from the four representative strains had slightly different electrophoretic mobilities (⌬DaХ800 Da); however, these were much smaller than those of the whole spiralins before formic acid hydrolysis (⌬DaХ8,000 Da). These results suggest that spiralin polymorphism in S. citri is not due to differences in posttranslational modification by palmitic acid and is certainly a structural property of the whole protein or could result from an unidentified posttranslational modification of spiralin.Among the mollicutes (i.e., wall-less eubacteria with low GϩC contents and small genomes), spiroplasmas are characterized by their helical morphology and motility. Spiroplasma citri, the first spiroplasma to have been cultured, is the causal agent of ''Stubborn'' disease of citrus (24) and affects many other plant species. S. citri also multiplies in various leafhoppers, which act as insect vectors. The spiroplasmas belong to the recently established order Entomoplasmatales, which also contains Entomoplasma and Mesoplasma species (31). All of these mollicutes are associated with arthropods, mainly insects. The spiroplasmas, like the mycoplasmas, ureaplasmas, mesoplasmas, and entomoplasmas, but unlike the acholeplasmas, use the triplet UGA, usually a stop codon, as a tryptophan codon (8,21).Spiralin is the most abundant membrane protein in S. citri (36). Its amphiphilic and antigenic properties (34, 38) and its membrane location and arrangement (30, 35) have been extensively studied. The spiralin gene has been identified, cloned, and expressed in Escherichia coli cells (19). Several forms of spiralin were produced in E. coli, including a major form with a slightly larger molecular mass than that of spiralin in S. citri. S. citri spiralin is free of tryptophan, and its gene has no UGA codon (6). This feature explains why the gene could be efficiently translated in E. coli at a time when it was not yet known that in spiroplasmas, UGA is not read as a stop codon but instead is read as a tryptophan codon. However, the function of spiralin in the spiroplasma cell remains undet...

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confidence: 62%

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Spiralin polymorphism in strains of Spiroplasma citri is not due to differences in posttranslational palmitoylation

et al. 1996

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Selective Acylation of Plasma Membrane Proteins of Mycoplasma mycoides subsp. mycoides SC, the Contagious Bovine Pleuropneumonia Agent

Jan

Fontenelle

Verrier

et al. 1996

Current Microbiology

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The plasma membrane of Mycoplasma mycoides subsp. mycoides SC (strain KH3J) contains over 160 polypeptides with apparent molecular masses ranging from 14 to 125 kDa and isoelectric point values (pIs) from 5 to 9. In vivo labeling with [14C]-fatty acids revealed about 35 acylated polypeptides including the two major components p42 and p65 and displaying pIs between 5.5 and 9.0, with a majority between 6.5 and 8. The amphiphilic nature of most of these acyl proteins was confirmed by Triton X-114 phase partitioning. Gas-liquid chromatography analyses showed that the order of preference for protein acylation was 16:0 > 18:2c > 18:1c > 18:0 > 14:0, with 16:0 being the major O-ester-bound fatty acyl chain and 18:2c the major N-linked chain. The presence of S-glycerylcysteine and a ratio of [O-ester-bound acyl chains + N-linked chains]/O-ester bound chains of approximately 1.2 in M. mycoides subsp. mycoides SC membrane proteins are consistent with a lipid modification similar to that occurring in lipoproteins of Gram-negative eubacteria that contain an N-terminal acyl S-glycerylcysteine.

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Inhibition of Spiralin Processing by the Lipopeptide Antibiotic Globomycin

Béven

Hénaff

Fontenelle

et al. 1996

Current Microbiology

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The cyclic lipopeptide globomycin, a specific inhibitor of signal-peptidase II (Lsp A), proved toxic for the mollicute Spiroplasma melliferum with a minimal inhibitory concentration (MIC) in the range 6.25-12.5 microM, about one order of magnitude higher (that is, less efficient) than bee-venom mellitin. SDS-PAGE analysis of cell proteins followed by immunolabeling ("Western blotting") and by crossed immunoelectrophoresis demonstrated that the cleavage of the prespiralin leader peptide was prevented by globomycin. Cell fractionation experiments showed that prespiralin was membrane bound and did not accumulate in the cytoplasm or in the culture medium. Furthermore, the use of the potential-sensitive fluorescent dye 3,3'-dipropyl-2,2'-thiadicarbocyanine iodide (diS-C3-[5]) revealed that, in contrast to valinomycin and mellitin, globomycin up to 30 microM has no effect on the electrical transmembrane potential of S. melliferum. This indicates that the toxicity of globomycin for spiroplasma cells is mainly if not exclusively owing to the inhibition of spiralin processing. Added to previously published data, these results suggest that spiralin and probably other lipoproteins of mollicutes are acylated and membrane targeted by a mechanism involving notably the processing of the prelipoprotein precursor by a type II, globomycin-sensitive signal peptidase.

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Palmitoylation of membrane proteins inSpiroplasma floricola

Cited by 4 publications

References 18 publications

Spiralin polymorphism in strains of Spiroplasma citri is not due to differences in posttranslational palmitoylation

Spiralin polymorphism in strains of Spiroplasma citri is not due to differences in posttranslational palmitoylation

Selective Acylation of Plasma Membrane Proteins of Mycoplasma mycoides subsp. mycoides SC, the Contagious Bovine Pleuropneumonia Agent

Inhibition of Spiralin Processing by the Lipopeptide Antibiotic Globomycin

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