PMID: 9188797May 22, 1997Paper

The hydrophobic region of signal peptides is involved in the interaction with membrane-bound SecA

Biochimica Et Biophysica Acta
H MoriS Mizushima

Abstract

The positive charges of signal peptides are important for the interaction with SecA, a translocation ATPase. To examine whether or not the hydrophobic region of signal peptides also interacts with SecA, we constructed model preproteins, proOmpF-Lpps, possessing no positively charged amino acid residues at the amino-terminus and different numbers of alanine/leucine residues in the hydrophobic region of signal peptides. When the hydrophobic stretch was sufficiently long, amino-terminal positively charged residues were not required for the translocation of preproteins across the cytoplasmic membrane of Escherichia coli both in vitro and in vivo. Chemical cross-linking between SecA and preproteins possessing no positively charged residues at the amino-terminus was observed only in the presence of liposomes containing acidic phospholipids. The degree of cross-linking increased as the length of the hydrophobic stretch increased irrespective of whether positively charged residues were present or not. A preprotein possessing no positively charged residues at the amino-terminus, which is competent in the presence of liposomes, competitively inhibited the cross-linking of wild-type proOmpF-Lpp with SecA under the same conditions. It is c...Continue Reading

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Citations

Mar 27, 2013·Applied Microbiology and Biotechnology·Kheng Oon LowRosli Md Illias
Sep 21, 2000·Molecular Microbiology·L Kourtz, D Oliver
Dec 5, 2006·Journal of Bacteriology·Changqi SunDebra A Kendall
Jul 28, 2005·The Journal of Biological Chemistry·Yi-Te Chou, Lila M Gierasch
Oct 28, 2019·Preparative Biochemistry & Biotechnology·Zahra HajihassanFarshid Zandsalimi
Apr 1, 2000·The Journal of Biological Chemistry·L WangD A Kendall
Mar 30, 2001·The Journal of Biological Chemistry·T L TriplettL M Gierasch
Feb 10, 2021·International Journal of Biological Macromolecules·Xiao GuoFufeng Liu

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