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The amino acid sequence of wheat histone H2B(12). A core histone with a novel repetitive N-terminal extension.
- Source :
- European Journal of Biochemistry; 5/2/88, Vol. 173 Issue 3, p547-554, 8p
- Publication Year :
- 1988
-
Abstract
- Two of the four electrophoretic histone H2B variants present in wheat embryos have been isolated. The complete primary structure of the H2B<subscript>(2)</subscript> variant has been deduced from sets of overlapping peptides generated by CNBr cleavage, Staphyloccocus aureus V8 protease, endoproteinase Arg-C, the post-proline cleaving enzyme, chymotrypsin and cleavage in dilute acid. A minimum of 17 peptides were required to establish the sequence. This variant has a blocked N terminus and comprises a total of 149 amino acids. The C-terminal two-thirds of the protein are highly homologous to vertebrate H2B. In contrast, the N-terminal third is entirely different and contains an N-terminal extension of 23 residues in which the sequence Ala-Glu-Lys or variants are repeated several times. This region is also highly homologous to the H2B from Tetrahymena pyriformis. It shows in addition similarities to wheat H2A<subscript>(1)</subscript> and bovine H1. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 173
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13774546
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1988.tb14033.x