Open AccessPrimary structure of histone H2B from gonads of the starfish Asterias rubens
Author(s) -
MARTINAGE Arlette,
BRIAND Gilbert,
DORSSELAER Alain,
TURNER Christopher H.,
SAUTIERE Pierre
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb08757.x
Subject(s) - starfish , histone h2b , histone , asterias , biochemistry , acetylation , biology , cleavage (geology) , amino acid , peptide sequence , chemistry , dna , gene , ecology , paleontology , fracture (geology)
The complete amino acid sequence (121 residues) of histone H2B from gonads of the starfish Asterias rubens has been established from structural data obtained essentially from large fragments generated by cleavage of histone H2B at aspartyl residues and by limited hydrolysis of the dimer H2A‐H2B with mouse submaxillary gland protease. No real sequence homology can be found between the amino‐terminal sequence (residues 1–21) of starfish and calf H2B. One non‐conservative substitution (serine‐32 in calf → lysine‐28 in starfish) leads to the presence of a cluster of eight basic residues (sequence 23 – 30) and to the disappearance of a potential site of phosphorylation. A particular structural feature of starfish histone H2B is the presence of N ‐dimethylproline at its aminoterminal end. By comparison with N ‐terminal acetylation, which is commonly found in histones, N‐terminal methylation is rarely observed. At the present time the functional significance of the N‐terminal methylation as well as that of the proline‐rich nature of the amino‐terminal sequence of the starfish histone H2B remain to be defined.