The nudeotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E. coil K12 (original) (raw)
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1 Present addresses: Judy Lin, Stanford Medical School, Stanford, CA94305; David Moore, Dept. of Biochemistry, University of California,San Francisco, CA 94143; Sarah Holder, Monsanto Chemical Corp.,St. Louis, MO.
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Department of Genetics, University of Wisconsin
Madison, WI 53706, USA
1 Present addresses: Judy Lin, Stanford Medical School, Stanford, CA94305; David Moore, Dept. of Biochemistry, University of California,San Francisco, CA 94143; Sarah Holder, Monsanto Chemical Corp.,St. Louis, MO.
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1 Present addresses: Judy Lin, Stanford Medical School, Stanford, CA94305; David Moore, Dept. of Biochemistry, University of California,San Francisco, CA 94143; Sarah Holder, Monsanto Chemical Corp.,St. Louis, MO.
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Zachary Burton, Richard R. Burgess, Judy Lin, David Moore, Sarah Holder, Carol A. Gross, The nudeotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E. coil K12, Nucleic Acids Research, Volume 9, Issue 12, 25 June 1981, Pages 2889–2903, https://doi.org/10.1093/nar/9.12.2889
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Abstract
We have determined the nudeotide sequence of the rpoD gene which codes for the sigma subunit of RNA polymerase from E. coli K12. The gene, which we formerly cloned as a Bindlll restriction fragment in the transducing phage, Charon 25, was recloned into several plasmids. We have determined a 2600 base pair DNA sequence which includes the entire structural gene for sigma. The resulting amino acid sequence agrees with previous information obtained about sigma including theamino acid composition, partial sequence data for the N-terminus, the highly acidic nature of the polypeptide, and the cleavage pattern at cysteines. The molecular weight of 70,263 daltons calculated for the 613 amino acid polypeptide is significantly lower than had been determined previously by SDS polyacrylamide gel analysis.
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