Literature DB >> 3371346

The primary structure of the histone H2A(2) type from wheat germ. A core histone type with both, N-terminal and C-terminal extensions.

J de Andrade Rodrigues1, W F Brandt, C Von Holt.   

Abstract

The histone H2A(2) type from wheat germ comprises at least two highly homologous isohistones with 151 amino acid residues. Microheterogeneity occurs mainly at the N-terminal and C-terminal regions. These isohistones have both N-terminal (7 amino acid residues) and C-terminal (15 amino acid residues) extensions relative to calf thymus histone H2A.

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Year:  1988        PMID: 3371346     DOI: 10.1111/j.1432-1033.1988.tb14035.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  4 in total

1.  Nucleotide sequence and expression of two cDNA coding for two histone H2B variants of maize.

Authors:  P Joanin; C Gigot; G Philipps
Journal:  Plant Mol Biol       Date:  1992-11       Impact factor: 4.076

2.  Phosphorylation of Plant H2A Histones.

Authors:  G R Green; L C Gustavsen; D L Poccia
Journal:  Plant Physiol       Date:  1990-07       Impact factor: 8.340

3.  H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3' processing signals.

Authors:  C Mannironi; W M Bonner; C L Hatch
Journal:  Nucleic Acids Res       Date:  1989-11-25       Impact factor: 16.971

4.  The organization structure and regulatory elements of Chlamydomonas histone genes reveal features linking plant and animal genes.

Authors:  S Fabry; K Müller; A Lindauer; P B Park; T Cornelius; R Schmitt
Journal:  Curr Genet       Date:  1995-09       Impact factor: 3.886

  4 in total

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