期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 103, 期 47, 页码 17927-17932出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0607025103
关键词
protein transport; secondary metabolism; Tat pathway; twin arginine signal peptide; proteome
资金
- Medical Research Council [G117/519] Funding Source: researchfish
- Medical Research Council [G117/519] Funding Source: Medline
- NIGMS NIH HHS [T32-GM07229, T32 GM007229] Funding Source: Medline
- MRC [G117/519] Funding Source: UKRI
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-Phi-Phi 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 polymer-degrading 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.
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