000151359 001__ 151359
000151359 005__ 20181203022000.0
000151359 0247_ $$2doi$$a10.1099/00221287-133-9-2411
000151359 022__ $$a0022-1287
000151359 02470 $$2PMID$$a3329213
000151359 037__ $$aARTICLE
000151359 245__ $$aAn unmodified form of the ColE2 lysis protein, an envelope lipoprotein, retains reduced ability to promote colicin E2 release and lysis of producing cells
000151359 260__ $$c1987
000151359 269__ $$a1987
000151359 336__ $$aJournal Articles
000151359 520__ $$aSite-directed mutagenesis was used to replace the codon for the N-terminal cysteine residue of pColE2-P9-encoded mature lysis protein (CelB) by an arginine codon. In contrast to the wild-type CelB protein, the product of the mutated gene, which has an altered signal peptidase cleavage site, was neither processed nor acylated. However, the mutant protein retained sufficient residual activity to cause partial, Mg2+-suppressible lysis and could activate envelope phospholipase A1-A2 and promote colicin release, albeit with reduced efficiency compared to the wild-type protein. We propose that the uncleaved signal peptide of the mutant protein acts as the functional equivalent of the fatty acyl groups normally linked to the N-terminal cysteine residue of the wild-type protein, thereby anchoring the protein in the cell envelope where it exerts its various effects.
000151359 6531_ $$aViral Proteins
000151359 700__ $$aPugsley, Anthony P.
000151359 700__ $$g177247$$aCole, Stewart T.$$0243892
000151359 773__ $$j133$$tJournal of general microbiology$$k9$$q2411-20
000151359 909C0 $$xU11742$$0252302$$pUPCOL
000151359 909CO $$pSV$$particle$$ooai:infoscience.tind.io:151359
000151359 917Z8 $$x148230
000151359 937__ $$aEPFL-ARTICLE-151359
000151359 973__ $$rREVIEWED$$sPUBLISHED$$aOTHER
000151359 980__ $$aARTICLE