@article{48c6e0ada3aa46bf84196c7aa23285f5,
title = "Positively charged lysine at the N-terminus of the signal peptide of the Escherichia coli alkaline phosphatase provides the secretion efficiency and is involved in the interaction with anionic phospholipids",
abstract = "Positively charged amino acid residues at the N-terminus of the signal peptide (SP) have been proposed to play a significant role in the initial step of protein secretion in bacteria. To test this hypothesis, Lys(-20) of the Escherichia coli alkaline phosphatase SP was replaced by other amino acid residues, and the effect of these substitutions on protein maturation was studied. The introduction of negatively charged and hydrophobic amino acids resulted in a decrease in secretion efficiency and impaired the SP-APL interaction, whereas His and Tyr had no significant effect. A structural analysis of the SP-APL interaction suggests that the positively charged Lyst(-20) determines the stability of the complex.",
keywords = "Alkaline phosphatase, Anionic phospholipid, Escherichia coli, Protein secretion, Signal peptide, Stereochemical analysis",
author = "Nesmeyanova, {Marina A.} and Karamyshev, {Andrew L.} and Karamysheva, {Zemphyra N.} and Kalinin, {Andrey E.} and Ksenzenko, {Vladimir N.} and Kajava, {Andrey V.}",
note = "Funding Information: We are grateful to J.H. Miller for kindly providing us with a collection of E. coli amber suppressors, to R. Fischer for providing the plasmid vector p15SK (+/−), to M. Shlyapnikov for oligonucleotide synthesis, to I. Sidorov for statistical analysis of the data, and to M. Bogdanov for design of an assay of glycerophosphate transfer from the membrane PG to arbutin. This work was supported by the Russian Foundation for Basic Research (Grant No. 96-04-48048), the Russian State Scientific Program `Modern methods of biological engineering' and was also made possible in part by an Award of the US Civilian Research and Development Foundation for the Independent States of the Former Soviet Union (Grant RBI-288). ",
year = "1997",
month = feb,
day = "17",
doi = "10.1016/S0014-5793(97)00052-5",
language = "English",
volume = "403",
pages = "203--207",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "FEBS letters",
number = "2",
}