A positive residue in the hydrophobic core of the Escherichia coli lipoprotein signal peptide suppresses the secretion defect caused by an acidic amino terminus.
Sung CY, Gennity JM, Pollitt NS, Inouye M.
Sung CY, et al. Among authors: inouye m.
J Biol Chem. 1992 Jan 15;267(2):997-1000.
J Biol Chem. 1992.
PMID: 1730688
Free article.
Replacement of the positively charged amino-terminal residues of prolipoprotein by acidic amino acids decreased the rate of precursor translocation (Inouye, S., Soberon, X., Franceschini, T., Nakamura, K., Itakura, K., and Inouye, M. (1982) Proc. ...Sci. U.S. …
Replacement of the positively charged amino-terminal residues of prolipoprotein by acidic amino acids decreased the rate of precursor transl …