TY - JOUR
T1 - Regulation of the glyoxylate bypass operon
T2 - Cloning and characterization of iclR
AU - Sunnarborg, A.
AU - Klumpp, D.
AU - Chung, T.
AU - LaPorte, D. C.
PY - 1990
Y1 - 1990
N2 - In Escherichia coli, expression of the glyoxylate bypass operon appears to be controlled, in part, by the product of iclR+. Mutations in iclR have been found to yield constitutive expression of this operon, suggesting that iclR+ encodes a repressor protein. We have cloned iclR+ by taking advantage of its tight genetic linkage with the glyoxylate bypass operon. The clone complemented a mutant allele of iclR in trans, restoring an inducible phenotype for this operon. Deletion analysis identified a region of ca. 900 base pairs that was necessary and sufficient for complementation. The nucleotide sequence of the insert was then determined. Translation of this sequence revealed an open reading frame capable of encoding a protein with M(r) 29,741 preceded by a potential Shine-Dalgarno ribosome-binding site. The deduced amino acid sequence includes a region at the amino terminus that may form a gelix-turn-helix motif, a structure found in many DNA-binding domains.
AB - In Escherichia coli, expression of the glyoxylate bypass operon appears to be controlled, in part, by the product of iclR+. Mutations in iclR have been found to yield constitutive expression of this operon, suggesting that iclR+ encodes a repressor protein. We have cloned iclR+ by taking advantage of its tight genetic linkage with the glyoxylate bypass operon. The clone complemented a mutant allele of iclR in trans, restoring an inducible phenotype for this operon. Deletion analysis identified a region of ca. 900 base pairs that was necessary and sufficient for complementation. The nucleotide sequence of the insert was then determined. Translation of this sequence revealed an open reading frame capable of encoding a protein with M(r) 29,741 preceded by a potential Shine-Dalgarno ribosome-binding site. The deduced amino acid sequence includes a region at the amino terminus that may form a gelix-turn-helix motif, a structure found in many DNA-binding domains.
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U2 - 10.1128/jb.172.5.2642-2649.1990
DO - 10.1128/jb.172.5.2642-2649.1990
M3 - Article
C2 - 2185227
AN - SCOPUS:0025355399
SN - 0021-9193
VL - 172
SP - 2642
EP - 2649
JO - Journal of bacteriology
JF - Journal of bacteriology
IS - 5
ER -