Primary Structure of Non-Histone Chromosomal Protein HMG2 Revealed by the Nucleotide Sequence

Hitoshi Shirakawa, Koh Ichiroh Tsuda, Michiteru Yoshida

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48 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)4419-4423
Number of pages5
JournalBiochemistry
Volume29
Issue number18
DOIs
Publication statusPublished - 1990 May 1

ASJC Scopus subject areas

  • Biochemistry

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