Localization of functional domains in E. coli K-12 outer membrane porins.
نویسندگان
چکیده
منابع مشابه
Comparison of Escherichia coli K-12 outer membrane protease OmpT and Salmonella typhimurium E protein.
The predicted amino acid sequence of OmpT, an Escherichia coli outer membrane protease, was found to be highly homologous to that predicted for the pgtE gene product of Salmonella typhimurium. In this paper, it is shown that pgtE codes for a protein functionally homologous to OmpT as judged by its ability to proteolyze T7 RNA polymerase and to localize in the outer membrane of E. coli.
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It is now well recognized that the outer membranes of gram-negative bacteria serve as molecular sieves which permit the passage of small hydrophilic molecules of sizes below a given cutoff, i.e., the exclusion limit (21, 27). This sieving property, which permits uptake of small substrate molecules but excludes potentially harmful enzymes and other large hydrophilic molecules, is due to a class ...
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Background & Objective: Brucellosis is an important zoonotic disease of economic significance. Brucella species are gram-negative, facultative intracellular bacteria, and are capable of replicating in the phagosomes of macrophages. They cause infection in several animal species and humans. Prevention of new diseases and diagnosis of cases infected with the organism are both essential for eradic...
متن کاملThe ultimate localization of an outer membrane protein of Escherichia coli K-12 is not determined by the signal sequence.
To study the role of the signal sequences in the biogenesis of outer membrane proteins, we have constructed two hybrid genes: a phoE-ompF hybrid gene, which encodes the signal sequence of outer membrane PhoE protein and the structural sequence of outer membrane OmpF protein, and a bla-phoE hybrid gene which encodes the signal sequence as well as 158 amino acids of the structural sequence of the...
متن کاملExport 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...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 1985
ISSN: 0261-4189
DOI: 10.1002/j.1460-2075.1985.tb03820.x