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Nucleic Acids Research, 1983, Vol. 11, No. 23 8509-8518
© 1983

MOLECULAR BIOLOGY

The DNA sequence of argI from Escherichia coli K12

David A. Bencini+, John E. Houghton, Timothy A. Hoover, Karen F. Foltermann, James R. Wild* and Gerard A. O'Donovan

Department of Biochemistry and Biophysics, Texas A&M University College Station, TX 77843, USA

*To whom communications should be addressed

Received June 24, 1983. Revised October 28, 1983. Accepted October 28, 1983.

The argI gene from E. coli K12 has been sequenced. It contains an open reading frame of 1002 bases which encodes a polypeptide of 334 amino adds. Three such polypeptides are required to form the functional catalytic trimer (c3) of ornithine transcarbamoylase (OTCase-1, EC 2.1.3.3). The molecular mass of the mature trimer deduced from the amino acid sequence is 114,465 daltons. An altered form of argI was produced when a 1.6 kilobase DdeI fragment was subcloned into the HincII site of plasmid pUC8 extending the open reading frame an additional 20 nucleotides. It has been previously reported that the amino-terminal region of the respective polypeptides of argI, argF, and pyrB of E. coli possessed significant homology. In contrast, the homologous promoter/operator regions of argI and argF did not appear to share any homologies with pyrB. However, a closer scrutiny of the nucleotide sequence Immediately preceding the pyrBI attenuator revealed a remarkable similarity to the argI and argF control region.

+Present address: Department of Chemistry, Gibbs Chemical Laboratories, Harvard University, Cambridge, MA 02138, USA.


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