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

Palacín, Arantxa; Fuente, Ricardo de la; Valle, Inmaculada; Rivas, Luis A.; Mellado, Rafael P.

doi:10.1099/mic.0.26313-0

Cited by 20 publications

(25 citation statements)

References 30 publications

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“…Agarase is encoded by the dagA gene, and the protein product bears an N-terminal signal peptide that contains an apparent twin-arginine motif ( Fig. 2A), despite earlier reports that it interacts with components of the signal recognition particle (24). Interestingly, colonies of the S. coelicolor tat mutants failed to sink into solid media suggesting DagA is perhaps a genuine Tat substrate.…”

Section: Tat-dependent Proteins Identified By 2d Gel Electrophoresis mentioning

confidence: 88%

The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor

Widdick

Dilks

Chandra³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

133

194

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The twin-arginine translocation (Tat) pathway is a protein transport system for the export of folded proteins. Substrate proteins are targeted to the Tat translocase by N-terminal signal peptides harboring a distinctive R-R-x-⌽-⌽ ''twin-arginine'' amino acid motif. Using a combination of proteomic techniques, the protein contents from the cell wall of the model Gram-positive bacterium Streptomyces coelicolor were identified and compared with that of mutant strains defective in Tat transport. The proteomic experiments pointed to 43 potentially Tat-dependent extracellular proteins. Of these, 25 were verified as bearing bona fide Tat-targeting signal peptides after independent screening with a facile, rapid, and sensitive reporter assay. The identified Tat substrates, among others, include polymerdegrading enzymes, phosphatases, and binding proteins as well as enzymes involved in secondary metabolism. Moreover, in addition to predicted extracellular substrates, putative lipoproteins were shown to be Tat-dependent. This work provides strong experimental evidence that the Tat system is used as a major general export pathway in Streptomyces.Protein transport ͉ secondary metabolism ͉ Tat pathway ͉ twin arginine signal peptide ͉ proteome

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Section: Tat-dependent Proteins Identified By 2d Gel Electrophoresis mentioning

confidence: 88%

The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor

Widdick

Dilks

Chandra³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

133

194

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“…Interestingly, a sequence that shows 91?6 % identity to 4?5S RNA in S. lividans (Palacin et al, 2003) is present 235 bp upstream from godI in the genome of strain TP-A0584 (Fig. 3a).…”

Section: Discussion Proposed Overall Biosynthetic Pathway Of Goadsporinmentioning

confidence: 99%

Cloning and characterization of the goadsporin biosynthetic gene cluster from Streptomyces sp. TP-A0584

et al. 2005

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The biosynthetic gene cluster of goadsporin, a polypeptide antibiotic containing thiazole and oxazole rings, was cloned from Streptomyces sp. TP-A0584. The cluster contains a structural gene, godA, and nine god (goadsporin) genes involved in post-translational modification, immunity and transcriptional regulation. Although the gene organization is similar to typical bacteriocin biosynthetic gene clusters, each goadsporin biosynthetic gene shows low homology to these genes. Goadsporin biosynthesis is initiated by the translation of godA, and the subsequent cyclization, dehydration and acetylation are probably catalysed by godD, godE, godF, godG and godH gene products. godI shows high similarity to the 54 kDa subunit of the signal recognition particle and plays an important role in goadsporin immunity. Furthermore, four goadsporin analogues were produced by site-directed mutagenesis of godA, suggesting that this biosynthesis machinery is used for the heterocyclization of peptides.

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“…The S. coelicolor genome is almost identical to that of S. lividans in which the secB gene appears to be lacking as well (San Roman M, and Mellado RP, unpublished results), thereby rendering a particular appeal to the study of the SRP complex. Studies carried out in our laboratory showed that the structure of the S. lividans SRP is coherent with a minimal functional SRP resembling that of E. coli and consists of Ffh and an 82-nt-long RNA [Palacín et al, 2003]. Co-immunoprecipitation studies confi rmed that the S. lividans SRP is involved in targeting secretory proteins [Palacín et al, 2003].…”

mentioning

confidence: 90%

“…Studies carried out in our laboratory showed that the structure of the S. lividans SRP is coherent with a minimal functional SRP resembling that of E. coli and consists of Ffh and an 82-nt-long RNA [Palacín et al, 2003]. Co-immunoprecipitation studies confi rmed that the S. lividans SRP is involved in targeting secretory proteins [Palacín et al, 2003].…”

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confidence: 90%

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The <i>Streptomyces lividans</i> Cytoplasmic Signal Recognition Particle Receptor FtsY Is Involved in Protein Secretion

Palomino¹,

Mellado²

2005

Microb Physiol

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The bacterial version of the mammalian signal recognition particle (SRP) and its receptor α-subunit (FtsY) is well conserved and essential to all known bacteria. In Gram-negative bacteria, the SRP pathway mediates a co-translational targeting of most inner membrane proteins. Additionally, in Streptomyces lividans, a Gram-positive bacterium, SRP also targets secretory proteins to the translocon. The role of S. lividans FtsY has been assessed in this work. Co-immunoprecipitation studies confirmed that FtsY is associated with the S. lividans SRP in the cytoplasm and that this complex also co-immunoprecipitated with pre-agarase, suggesting that the SRP receptor is involved in SRP-mediated targeting of secretory proteins in S. lividans. Furthermore, the SRP remains attached for the most part to the cellular membrane when the cleavage of pre-secretory proteins is severely reduced in a strain lacking the gene coding for the major type-I signal peptidase.

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

Cited by 20 publications

References 30 publications

The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor

The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor

Cloning and characterization of the goadsporin biosynthetic gene cluster from Streptomyces sp. TP-A0584

The <i>Streptomyces lividans</i> Cytoplasmic Signal Recognition Particle Receptor FtsY Is Involved in Protein Secretion

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