Ralstonia eutropha TF93 Is Blocked in Tat-Mediated Protein Export

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Ralstonia eutropha TF93 is blocked in tat-mediated protein export.

Ralstonia eutropha (formerly Alcaligenes eutrophus) TF93 is pleiotropically affected in the translocation of redox enzymes synthesized with an N-terminal signal peptide bearing a twin arginine (S/T-R-R-X-F-L-K) motif. Immunoblot analyses showed that the catalytic subunits of the membrane-bound [NiFe] hydrogenase (MBH) and the molybdenum cofactor-binding periplasmic nitrate reductase (Nap) are m...

متن کامل

Escherichia coli strains blocked in Tat-dependent protein export exhibit pleiotropic defects in the cell envelope.

The Tat system is a recently discovered protein export pathway that serves to translocate folded proteins, often containing redox cofactors, across the bacterial cytoplasmic membrane. Here we report that tat strains are associated with a mutant cell septation phenotype, where chains of up to 10 cells are evident. Mutant strains are also hypersensitive to hydrophobic drugs and to lysis by lysozy...

متن کامل

A putative monofunctional glycosyltransferase is expressed in Ralstonia eutropha.

A gene, mgt, encoding a protein homologous to the N-terminal module of class A high-molecular-mass penicillin-binding proteins was identified in Ralstonia eutropha. By using specific antibodies, the corresponding Mgt protein was detected in association with the membrane, confirming that the N-terminal hydrophobic segment functioned as a membrane anchor. A derivative in which the hydrophobic seq...

متن کامل

Formate dehydrogenase from Ralstonia eutropha

1 Spectroscopic and kinetic properties of the molybdenum-containing, NAD+-dependent formate dehydrogenase from Ralstonia eutropha. Dimitri Niks, Jayant Duvvuru, Miguel Escalona, and Russ Hille Department of Biochemistry, University of California, Riverside, Riverside, CA 92521 Running title: Formate dehydrogenase from Ralstonia eutropha To whom correspondence should be addressed: Prof. Russ Hil...

متن کامل

The hydrogen-sensing apparatus in Ralstonia eutropha.

Molecular hydrogen is widely used by microorganisms as a source of energy. One of the best studied aerobic hydrogen oxidizers, the beta-proteobacterium Ralstonia eutropha (formerly Alcaligenes eutrophus), harbors two distinct [NiFe]-hydrogenases which catalyze the heterolytic cleavage of H2 into 2H+ and 2e-. The genes encoding the hydrogenase subunits are arranged in two large operons together ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 2000

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.182.3.581-588.2000