Production of functional rat HMG1 protein in Escherichia coli

Gene. 1991 Aug 15;104(2):271-5. doi: 10.1016/0378-1119(91)90261-9.

Abstract

High-mobility group-1 protein (HMG1) was produced in Escherichia coli under the control of the T7 promoter/T7 RNA polymerase system. The protein can be produced and purified with yields similar to those obtained from animal tissues. HMG1 purified from E. coli is homogeneous and capable of selectively binding cruciform DNA, indicating that post-translational processing of vertebrate HMG1 is not necessary for its DNA-binding ability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA / metabolism
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Escherichia coli / genetics
  • High Mobility Group Proteins / genetics*
  • High Mobility Group Proteins / isolation & purification
  • Molecular Sequence Data
  • Plasmids
  • Protein Processing, Post-Translational
  • Rats

Substances

  • DNA-Binding Proteins
  • High Mobility Group Proteins
  • DNA

Associated data

  • GENBANK/M63853