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Nucleic Acids Research, 1985, Vol. 13, No. 14 5297-5315
© 1985

Articles

Structural features of the hisT operon of Escherichia coli K-12

Peggy J. Arps, Christopher C. Marvel1,+, Beth C. Rubin, Dean A. Tolan1, Edward E. Penhoet1 and Malcolm E. Winkler*

Department of Molecular Biology, Northwestern University Medical School Chicago, IL 60611 1Department of Biochemistry, University of California Berkeley, CA 94720, USA

*To whom correspondence should be addressed

Received April 25, 1985. Revised June 17, 1985. Accepted June 19, 1985.

The DNA sequence of a 2.3-kilobase segment of the E. coli hisT operon was determined. Analysis of the sequence indicated that the upstream gene in the operon encodes a 36,364-dalton polypeptide, which runs aberrantly on SDS-poly acrylamide gels. The distal hisT gene encodes the tRNA modification enzyme, pseudouridine synthase I, which was shown to have a polypeptide molecular mass of 30,399 daltons. The DNA sequence was consistent with the phenotypes and hisT expression of mutant operons. Analysis of the sequence and genetic complementation experiments demonstrated that the upstream and hisT genes are evolutionarily, structurally, and functionally unrelated; however, translation signals for the two genes overlap, which is consistent with genetic evidence suggesting translational coupling. Codon usage in the upstream gene is radically different from the hisT gene and may underlie the differential expression observed from the operon. Gene-inactivation experiments and S1-mapping of in vivo transcripts indicated that the operon contains an additional upstream gene. S1-mapping experiments also confirmed the presence of an internal promoter, which might be stringently controlled. Taken together, these results show that the structure of the hisT operon is complex and suggest that the operon might be regulated at several levels.

+ Present address: Naval Biosciences Laboratory, University of California, Berkeley, CA 94720


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