Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli.-Reference-Cited by-同舟云学术

Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli.

Published:1991-12 Issue:36 Volume:266 Page:24420-24427
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cabelli R.J.,Dolan K.M.,Qian L.P.,Oliver D.B.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.

2. SecA, an essential component of the secretory machinery of Escherichiacoli, exists as homodimer

3. Cabelli, R. J. (1991) Biochemical Characterization of the Role of SecA Protein in Protein Export in Escherichice coli. Ph.D. thesis, State University of New York, Stony Brook, New York

4. SecA protein is required for secretory protein translocation into E. coli membrane vesicles

5. [21] β-Galactosidase gene fusions for analyzing gene expression in Escherichia coli and yeast

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