The primary structure of the major isoform (H1.1) of histone H1 from the nematode Caenorhabditis elegans.
The complete primary structure of the major isoform (H1.1) of histone H1 from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 207 amino acids and has a blocked N-terminus. The nematode histone shows rather little sequence identity when compared with proteins of the H1 family derived from other organisms. However, the main characteristic features of H1 molecules have been well conserved: a tripartite domain structure consisting of a central hydrophobic core of about 80 residues, flanked by an N-terminal domain which is somewhat acidic at the very N-terminus, but very basic further on, and a long C-terminal domain very rich in lysine, alanine and proline. Several repeat structures, including a twice (with modification)-repeated and well-conserved phosphorylation site, can be recognized in this region. The presence of O-phosphoserine at these sites could not be demonstrated, however.
Vanfleteren
J R
JR
Laboratorium voor Morfologie en Systematiek der Dieren, Rijksuniversiteit Gent, Belgium.
Van Bun
S M
SM
Van Beeumen
J J
JJ
D000595:Amino Acid Sequence; D000818:Animals; D002107:Caenorhabditis / Q000032:analysis*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis
D006657:Histones; D010446:Peptide Fragments