The primary structure of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans.
The complete amino acid sequence of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 190 residues and has a blocked N-terminus. Histone subtype H1.2 is 17 residues shorter than the major isoform H1.1, mainly as the result of deletions of short peptide fragments. Considerable divergence from isoform H1.1 has occurred in the N-terminal domain and the very C-terminus of the molecule, but the central globular domain and most of the C-terminal domain, including two potential phosphorylation sites, have been well conserved. Secondary-structure predictions for both H1 isoforms reveal a high potential for helix formation in the N-terminal region 1-33 of isoform H1.1 whereas the corresponding region in isoform H1.2 has low probability of being found in alpha-helix. No major differences in secondary structure are predicted for other parts of both H1 subtypes. The aberrant conformation of isoform H1.2 may be indicative of a significantly different function.
Laboratorium voor Morfologie en Systematiek der Dieren, Rijksuniversiteit Gent, Belgium.
J R
JR
Vanfleteren
S M
SM
Van Bun
I
I
De Baere
J J
JJ
Van Beeumen
D000595:Amino Acid Sequence; D000818:Animals; D002107:Caenorhabditis / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D006657:Histones / Q000302:isolation & purification; D008969:Molecular Sequence Data; D013379:Substrate Specificity
D006657:Histones; D010450:Endopeptidases