| Autor: |
Jongbloed, JDH, Martin, U, Antelmann, H, Hecker, M, Tjalsma, H, Venema, G, Bron, S, van Dijl, JM |
| Přispěvatelé: |
Groningen Biomolecular Sciences and Biotechnology, Cardiovascular Centre (CVC), Translational Immunology Groningen (TRIGR) |
| Jazyk: |
angličtina |
| Rok vydání: |
2000 |
| Předmět: |
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| Zdroj: |
The Journal of Biological Chemistry, 275(52), 41350-41357. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| ISSN: |
0021-9258 |
| Popis: |
The recent discovery of a ubiquitous translocation pathway, specifically required for proteins with a twin-arginine motif in their signal peptide, has focused interest on its membrane-bound components, one of which is known as TatC. Unlike most organisms of which the genome has been sequenced completely, the Gram-positive eubacterium Bacillus subtilis contains two tatC-like genes denoted tatCd and tatCy. The corresponding TatCd and TatCy proteins have the potential to be involved in the translocation of 27 proteins with putative twin-arginine signal peptides of which similar to6-14 are likely to be secreted into the growth medium. Using a proteomic approach, we show that PhoD of B. subtilis, a phosphodiesterase belonging to a novel protein family of which all known members are synthesized with typical twin-arginine signal peptides, is secreted via the twin-arginine translocation pathway. Strikingly, TatCd is of major importance for the secretion of PhoD, whereas TatCy is not required for this process. Thus, TatC appears to be a specificity determinant for protein secretion via the Tat pathway, Based on our observations, we hypothesize that the TatC determined pathway specificity is based on specific interactions between TatC-like proteins and other pathway components, such as TatA, of which three paralogues are present in B. subtilis. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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