Specific Targeting of the Metallophosphoesterase YkuE to the Bacillus Cell Wall Requires the Twin-arginine Translocation System |
| |
Authors: | Carmine G Monteferrante Marcus Miethke René van der Ploeg Corinna Glasner Jan Maarten van Dijl |
| |
Affiliation: | From the Department of Medical Microbiology, University of Groningen and University Medical Center Groningen, Hanzeplein 1, P. O. Box 30001, 9700 RB Groningen, The Netherlands and. |
| |
Abstract: | The twin-arginine translocation (Tat) pathway is dedicated to the transport of fully folded proteins across the cytoplasmic membranes of many bacteria and the chloroplast thylakoidal membrane. Accordingly, Tat-dependently translocated proteins are known to be delivered to the periplasm of Gram-negative bacteria, the growth medium of Gram-positive bacteria, and the thylakoid lumen. Here, we present the first example of a protein, YkuE of Bacillus subtilis, that is specifically targeted by the Tat pathway to the cell wall of a Gram-positive bacterium. The cell wall binding of YkuE is facilitated by electrostatic interactions. Interestingly, under particular conditions, YkuE can also be targeted to the cell wall in a Tat-independent manner. The biological function of YkuE was so far unknown. Our present studies show that YkuE is a metal-dependent phosphoesterase that preferentially binds manganese and zinc. |
| |
Keywords: | Bacillus Metalloenzymes Protein Export Protein Secretion Protein Translocation Tat Twin-arginine Translocation System Cell Wall |
本文献已被 PubMed 等数据库收录! |
|