000151389 001__ 151389
000151389 005__ 20181203022001.0
000151389 022__ $$a0014-2956
000151389 02470 $$2PMID$$a391567
000151389 0247_ $$2doi$$a10.1111/j.1432-1033.1979.tb06263.x
000151389 037__ $$aARTICLE
000151389 245__ $$aProduction of a soluble form of fumarate reductase by multiple gene duplication in Escherichia coli K12
000151389 269__ $$a1979
000151389 260__ $$c1979
000151389 336__ $$aJournal Articles
000151389 520__ $$a1. Ampicillin-hyperresistant mutants of Escherichia coli K12 bearing multiple gene duplications in the ampC (beta-lactamase) gene region of the chromosome overproduced at least six proteins with molecular weights 97,000, 80,000, 72,000, 49,000, 33,000 and 26,500 during anaerobic growth. All but two of the proteins (80,000-Mr and 49,000-Mr) were also overproduced during aerobic growth. The distribution of the proteins in soluble and particulate cell fractions was investigated. 2. The 33,000-Mr and 72,000-Mr components were identified as beta-lactamase and the amp-linked frdA gene product, fumarate reductase, respectively. Co-sedimentation of the 26,500-Mr component with the fumarate reductase suggested that the smaller protein could be functionally related to the reductase. The lack of correspondence between the amplified proteins and the products of other amp-linked genes, aspA and mop(groE), indicated that these genes are not included in the repetitive sequence. 3. Fumarate reductase activities were amplified up to 32-fold by the multiple gene duplications. Two forms of fumarate reductase were produced: particulate (membrane-bound) and soluble (cytoplasmic). Production of the soluble form occurred when the binding capacity of the membrane was saturated. Both forms of fumarate reductase were enzymically active but the soluble form was readily inactivated under assay conditions.
000151389 700__ $$0243892$$g177247$$aCole, S T
000151389 700__ $$aGuest, J R
000151389 773__ $$j102$$tEuropean journal of biochemistry / FEBS$$k1$$q65-71
000151389 909C0 $$xU11742$$0252302$$pUPCOL
000151389 909CO $$pSV$$particle$$ooai:infoscience.tind.io:151389
000151389 937__ $$aEPFL-ARTICLE-151389
000151389 973__ $$rREVIEWED$$sPUBLISHED$$aOTHER
000151389 980__ $$aARTICLE