Export of FepA::PhoA fusion proteins to the outer membrane of Escherichia coli K-12

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

Export of FepA::PhoA fusion proteins to the outer membrane of Escherichia coli K-12.

A library of fepA::phoA gene fusions was generated in order to study the structure and secretion of the Escherichia coli K-12 ferric enterobactin receptor, FepA. All of the fusion proteins contained various lengths of the amino-terminal portion of FepA fused in frame to the catalytic portion of bacterial alkaline phosphatase. Localization of FepA::PhoA fusion proteins in the cell envelope was d...

متن کامل

An outer membrane protein (OmpA) of Escherichia coli K-12 undergoes a conformational change during export.

Pulse-chase experiments were performed to follow the export of the Escherichia coli outer membrane protein OmpA. Besides the pro-OmpA protein, which carries a 21-residue signal sequence, three species of ompA gene products were distinguishable. One probably represented an incomplete nascent chain, another the mature protein in the outer membrane, and the third, designated imp-OmpA (immature pro...

متن کامل

Export and localization of N-terminally truncated derivatives of Escherichia coli K-12 outer membrane protein PhoE.

To identify export and sorting information in outer membrane protein PhoE of Escherichia coli K-12, a set of deletions was created, resulting in the removal of N-terminal amino acids of the mature protein. Pulse-chase experiments revealed that some mutant proteins were slowly or not at all processed, but there was not correlation between processing rate and the extent of the deletions. The unpr...

متن کامل

Iron-regulated outer membrane proteins of Escherichia coli K-12 and mechanism of action of catechol-substituted cephalosporins.

Selected aminothiazolyl-oxime cephalosporin congeners substituted at C-3' with a catechol moiety were used to probe the basis of the enhanced antibacterial activity against Escherichia coli K-12 often associated with chemical modifications of this type. Evidence is presented for a tonB-dependent illicit transport of the compounds across the outer membrane of E. coli K-12, the process involving ...

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: 1989

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.171.11.5894-5900.1989