Stabilising and destabilising modifications of cysteines in theE. coliouter membrane porin protein OmpC
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چکیده
منابع مشابه
OmpC-like porin from Serratia rnarcescens
Department of Microbiology, University of Manitoba, Winnipeg, Manitoba, Canada R3T 2N2 An oligonucleotide that encodes the N-terminal portion of a 41 kDa porin of Serratia marcescens was used to probe S. marcescens UOC-51 genomic DNA. An 11 kb EcoRl fragment which hybridized with the oligonucleotide was subcloned into Escherichia coli, examined for expression, and sequenced. The product express...
متن کاملOverexpression, refolding, and purification of the major immunodominant outer membrane porin OmpC from Salmonella typhi: characterization of refolded OmpC.
The major immunodominant integral outer membrane protein C (OmpC) from Salmonella typhi Ty21a was overexpressed, without the signal peptide, in Escherichia coli. The protein aggregates as inclusion bodies (IBs) in the cytoplasm. OmpC from IBs was solubilized with 4 M urea and refolded. This involved rapid dilution of unfolded OmpC into a refolding buffer containing polyoxyethylene-9-lauryl ethe...
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هدف از آزمایش اول بررسی اثر سطوح مختلف سریسین [0 (control), 0.1, 0.5, 1.0, 2.5 %] افزوده شده به محیط , ivm بر cumulus cell expansion، بلوغ هسته و توسعه متوالی جنین، در گوسفندان نژاد سنجابی در فصل تولید مثلی می باشد. از سرگیری میوز به وسیله خارج شدن اولین پولار بادی اندازه گیری و هم چنین درصد رسیدن جنین های دو سلولی به مرحله کلیواژ و بلاستوسیت نیز به عنوان نشانه ای از میزان شایستگی توسعه اولیه ج...
Export-defective lamB protein is a target for translational control caused by ompC porin overexpression.
Overexpression of OmpC protein from an inducible plasmid vector reduced the amount of the precursor form of LamB protein in LamB signal sequence mutants. The stability of the precursor form of LamB protein was not affected, indicating that the effect of OmpC overexpression was on the synthesis of the precursor rather than on degradation. These results indicate that a functional signal sequence ...
متن کاملCharacterization of SH groups in porin of bovine heart mitochondria. Porin cysteines are localized in the channel walls.
Porin from bovine heart mitochondria contains probably two cysteines (Cys126 and Cys230 in human porin, Kayser, H., Kratzin, H. D., Thinnes, F. P., Götz, H., Schmidt, W. E., Eckart, K. & Hilschmann, N. (1989) Biol. Chem. Hoppe-Seyler 370, 1265-1278). Reduced and oxidized forms of these cysteines were investigated in purified protein and in intact mitochondria using the agents dithioerythritol, ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1997
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(97)00690-x