Negatively charged amino acid residues play an active role in orienting the Sec-independent Pf3 coat protein in theEscherichia coliinner membrane
Author:
Affiliation:
1. Department of Microbiology, University of Karlsruhe; D-76128 Karlsruhe Germany
2. Department of Chemistry, The Ohio State University; Columbus OH 43210 USA
Publisher
Wiley
Subject
General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience
Reference33 articles.
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2. Positively charged residues influence the degree of SecA dependence in protein translocation across the E.coli inner membrane;Andersson;FEBS Lett,1994
3. Different positively charged amino acids have similar effects on the topology of a polytopic transmembrane protein in Escherichia coli;Andersson;J Biol Chem,1992
4. Charged residues are major determinants of the transmembrane orientation of a signal-anchor sequence;Beltzer;J Biol Chem,1991
5. Translocation of N-terminal tails across the plasma membrane;Cao;EMBO J,1994
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