Molecular and General Genetics MGG

, Volume 217, Issue 1, pp 126–131

Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coli

  • Byron E. Froman
  • Robert C. Tait
  • L. D. Gottlieb
Article

DOI: 10.1007/BF00330951

Cite this article as:
Froman, B.E., Tait, R.C. & Gottlieb, L.D. Mol Gen Genet (1989) 217: 126. doi:10.1007/BF00330951

Summary

The nucleotide sequence of the gene encoding the glycolytic enzyme phosphoglucose isomerase (PGI) from Escherichia coli is presented. The gene encodes a polypeptide of 549 amino acids. The transcriptional start point of the gene was determined and found to lie within a consensus promoter region. The amino acid sequence derived from the E. coli PGI gene can be aligned without insertions or deletions to the predicted amino acid sequence of a nuclear-encoded chloroplast isozyme of PGI from a higher plant, and the two sequences have a similarity of 87.6%. The amino acid sequence similarity between E. coli and that predicted from cDNA sequences for mouse and pig PGI is approximately 65%.

Key words

Glycolytic enzymeMolecular evolution

Abbreviations

Ap

ampicillin

aa

amino acid(s)

nt

nucleotide(s)

ORF

open reading frame

PGI

phosphoglucose isomerase

MW

molecular weight

kDa

kilo Daltons

ss

single strand

RF

replicative form

LB

Luria broth

kb

kilobasepairs

Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • Byron E. Froman
    • 1
  • Robert C. Tait
    • 1
  • L. D. Gottlieb
    • 1
  1. 1.Department of GeneticsUniversity of CaliforniaDavisUSA