Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: sequential assignment and secondary structure.

TitleHomo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: sequential assignment and secondary structure.
Publication TypeJournal Article
Year of Publication1993
AuthorsCerf, C., G. Lippens, S. Muyldermans, A. Segers, V. Ramakrishnan, S. J. Wodak, K. Hallenga, and L. Wyns
JournalBiochemistry
Volume32
Issue42
Pagination11345-51
Date Published1993 Oct 26
ISSN0006-2960
KeywordsAmino Acid Sequence, Animals, Chickens, Erythrocytes, Genes, Synthetic, Histones, Magnetic Resonance Spectroscopy, Models, Structural, Molecular Sequence Data, Protein Structure, Secondary, Recombinant Proteins
Abstract

A recombinant 75 amino acid polypeptide corresponding to the globular domain of the chicken histone H1 (GH1) has been studied by 1H homonuclear and 1H-15N heteronuclear 2D NMR spectroscopy. Sequential assignment of the backbone and beta-proton resonances has enabled us to determine the secondary structure of GH1. It was found to consist of three helical regions (T7-S17, L25-Y37, E40-K56) and probably a beta-hairpin (L59-L73). This structure is similar to the structure of the globular domain of histone H5 (GH5) obtained both by NMR spectroscopy [Zarbock et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7628-7632; Clore et al. (1987) EMBO J. 6, 1833-1842] and by X-ray crystallography [Ramakrishnan et al. (1993) Nature 362, 219-223]. The beta-hairpin as suggested for GH1 is also present in the X-ray structure of GH5 but has not been reported for the NMR structure of GH5.

Alternate JournalBiochemistry
PubMed ID8218199
Grant ListGM42796 / GM / NIGMS NIH HHS / United States