Primary structure of non-histone chromosomal protein HMG2 revealed by the nucleotide sequence

Biochemistry. 1990 May 8;29(18):4419-23. doi: 10.1021/bi00470a022.


The isolation and sequencing of a cDNA clone for the entire sequence of pig thymus non-histone protein HMG2 are described. cDNA the size of 1153 nucleotides contains an open reading frame of 627 nucleotides. The 5'-untranslated region of 146 nucleotides is extremely rich in GC residues whereas the 3'-untranslated region of 380 nucleotides is rich in AT residues. The open reading frame encodes 209 amino acids, which contain a unique continuous run of 23 acidic amino acids at the C-terminal. The deduced amino acid sequence is 79% homologous to that of HMG1 protein from the same source which we reported [Tsuda, K., Kikuchi, M., Mori, K., Waga, S., & Yoshida, M. (1988) Biochemistry 27, 6159-6163]. In addition, the hydropathy index profiles of both proteins are very similar, supporting that they have similar structural features. Northern analysis of poly(A+) RNA reveals that a single-sized mRNA codes for HMG2 protein. Southern analysis suggests that the HMG2 coding gene is homogeneous within the pig thymus genome.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Southern
  • Cloning, Molecular
  • DNA / genetics
  • DNA / isolation & purification
  • Gene Library
  • High Mobility Group Proteins / genetics*
  • Molecular Sequence Data
  • Molecular Weight
  • Protein Conformation
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid
  • Swine
  • Thymus Gland / metabolism


  • High Mobility Group Proteins
  • DNA

Associated data

  • GENBANK/J02895