000151375 001__ 151375
000151375 005__ 20181203022000.0
000151375 022__ $$a0014-2956
000151375 02470 $$2PMID$$a6349993
000151375 0247_ $$2doi$$a10.1111/j.1432-1033.1983.tb07594.x
000151375 037__ $$aARTICLE
000151375 245__ $$aCloning and molecular characterization of the ompA gene from Salmonella typhimurium
000151375 269__ $$a1983
000151375 260__ $$c1983
000151375 336__ $$aJournal Articles
000151375 520__ $$aThe ompA gene from Salmonella typhimurium, encoding a major heat-modifiable protein of the outer membrane, has been cloned and extensively characterized. When expressed in Escherichia coli the gene directs the synthesis of an OmpA protein which is functionally and topologically indistinguishable from that made in S. typhimurium, thus indicating that export and membrane incorporation are very similar in the two organisms. The S. typhimurium protein effectively substitutes for the E. coli polypeptide in F-dependent conjugation and in the uptake of certain colicins, although it cannot serve as the receptor for the OmpA-specific phages K3 and TuII. On examination of the primary sequence of the protein, predicted from the nucleotide sequence of its gene, it was found that those domains likely to be exposed on the cell surface were significantly different to the corresponding regions of the E. coli polypeptide. These differences in the structure of the two proteins have been used to interpret differences in their biological activities.
000151375 6531_ $$aCloning, Molecular
000151375 700__ $$aFreudl, R
000151375 700__ $$0243892$$aCole, S T$$g177247
000151375 773__ $$j134$$k3$$q497-502$$tEuropean journal of biochemistry / FEBS
000151375 909C0 $$0252302$$pUPCOL$$xU11742
000151375 909CO $$ooai:infoscience.tind.io:151375$$pSV$$particle
000151375 937__ $$aEPFL-ARTICLE-151375
000151375 973__ $$aOTHER$$rREVIEWED$$sPUBLISHED
000151375 980__ $$aARTICLE