The effect of Srb, a homologue of the mammalian SRP receptor α-subunit, on Bacillus subtilis growth and protein translocation

Oguro, Ami; Kakeshita, Hiroshi; Takamatsu, Hiromu; Nakamura, Kouji; Yamane, Kunio

doi:10.1016/0378-1119(96)00181-3

Cited by 35 publications

(55 citation statements)

References 16 publications

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“…Moreover, neither B. subtilis nor S. lividans have an equivalent to the E. coli SecB protein. The B. subtilis SRP system seems able to substitute the SecB deficiency targeting membrane and secretory proteins (Oguro et al, 1996); therefore, the identification of the SRP components in S. lividans and the search as to whether they were involved in protein secretion was an obvious task.…”

Section: Discussionmentioning

confidence: 99%

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Streptomyces lividans contains a minimal functional signal recognition particle that is involved in protein secretion

et al. 2003

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The bacterial version of the mammalian signal recognition particle (SRP) is well conserved and essential to all known bacteria. The genes for the Streptomyces lividans SRP components have been cloned and characterized. FtsY resembles the mammalian SRP receptor and the S. lividans SRP consists of Ffh, a homologue of the mammalian SRP54 protein, and scRNA, which is a small size RNA of 82 nt in length. Co-immunoprecipitation studies confirmed that Ffh and scRNA are probably the only components of the S. lividans SRP and that pre-agarase can co-immunoprecipitate with Ffh, suggesting that the SRP is involved in targeting secretory proteins.

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Section: Discussionmentioning

confidence: 99%

“…B. subtilis does not seem to have a SecB protein and the signal peptides of the B. subtilis secretory proteins seem to be more hydrophobic and longer than those of E. coli. Thus, the B. subtilis SRP system may be responsible for the targeting of both membrane and secretory proteins (Oguro et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Streptomyces lividans contains a minimal functional signal recognition particle that is involved in protein secretion

et al. 2003

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“…To confirm that the observed phenotypes were due to disruption of smc and not to possible polar effects on the downstream srb gene (Oguro et al 1996), we used a plasmid, pDL53, that contains a fragment extending from bp 1274 of smc to bp 58 of srb. Integration of this plasmid into the chromosome should affect expression of srb exactly the same as integration of pRB9 and pDL55 but should not disrupt smc.…”

Section: Plasmids and Strainsmentioning

confidence: 99%

“…subtilis, along with many other bacterial species (but not E. coli or H. influenzae), contains a homolog of the eukaryotic Smc (structural maintenance of chromosomes) proteins (Oguro et al 1996). Several eukaryotes have multiple smc genes, and eukaryotic Smc proteins play a role in chromosome condensation, pairing, and/or segregation (for review, see Hirano et al 1995;Koshland and Strunnikov 1996;Heck 1997).…”

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Characterization of a prokaryotic SMC protein involved in chromosome partitioning

Britton

Lin²,

Grossman³

1998

Genes & Development

263

298

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smc of Bacillus subtilis encodes a homolog of eukaryotic SMC proteins involved in chromosome condensation, pairing, and partitioning. A null mutation in B. subtilis smc caused a temperature-sensitive-lethal phenotype in rich medium. Under permissive conditions, the mutant had abnormal nucleoids, ∼10% of the cells were anucleate, and assembly of foci of the chromosome partitioning protein Spo0J was altered. In combination with a null mutation in spo0J, the smc mutation caused a synthetic phenotype; cell growth was slower and ∼25% of the cells were anucleate. Our results demonstrate that the B. subtilis Smc protein, like its eukaryotic counterpart, plays an important role in chromosome structure and partitioning.

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Compensatory effect of the minor Streptomyces lividans type I signal peptidases on the SipY major signal peptidase deficiency as determined by extracellular proteome analysis

et al. 2006

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The developmentally complex bacterium Streptomyces lividans has the ability to produce and secrete a significant amount of protein and possesses four different type I signal peptidase genes (sipW, sipX, sipY and sipZ) that are unusually clustered in its chromosome. 2-DE and subsequent MS of extracellular proteins showed that proteins with typical export signals for type I and type II signal peptidases are the main components of the S. lividans secretome. Secretion of extracellular proteins is severely reduced in a strain deficient in the major type I signal peptidase (SipY). This deficiency was efficiently compensated by complementation with any of the other three signal peptidases as deduced from a comparison of the corresponding 2-D PAGE patterns with that of the wild-type strain.

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The effect of Srb, a homologue of the mammalian SRP receptor α-subunit, on Bacillus subtilis growth and protein translocation

Cited by 35 publications

References 16 publications

Streptomyces lividans contains a minimal functional signal recognition particle that is involved in protein secretion

Streptomyces lividans contains a minimal functional signal recognition particle that is involved in protein secretion

Characterization of a prokaryotic SMC protein involved in chromosome partitioning

Compensatory effect of the minor Streptomyces lividans type I signal peptidases on the SipY major signal peptidase deficiency as determined by extracellular proteome analysis

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