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

TY - JOUR

T1 - The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor

AU - Widdick, David

AU - Dilks, Kieran

AU - Chandra, Govind

AU - Bottrill, Andrew

AU - Naldrett, Mike

AU - Pohlschroder, Mechthild

AU - Palmer, Tracy

A2 - Beckwith, Jonathan

N1 - dc.publisher: National Academy of Sciences

PY - 2006

Y1 - 2006

N2 - 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-F-F “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.

AB - 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-F-F “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.

KW - Protein transport

KW - Secondary metabolism

KW - Tat pathway

KW - Twin arginine signal peptide

KW - Proteome

U2 - 10.1073/pnas.0607025103

DO - 10.1073/pnas.0607025103

M3 - Article

C2 - 17093047

SN - 0027-8424

VL - 103

SP - 17927

EP - 17932

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 47

ER -