Open AccessThe Primary Structure of Histone H1 from Sperm of the Sea Urchin Parechinus angulosus
Author(s) -
STRICKLAND Walter N.,
STRICKLAND Marie,
BRANDT Wolf F.,
HOLT Claus,
LEHMANN Arnold,
WITTMANNLIEBOLD Brigitte
Publication year - 1980
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1980.tb04460.x
Subject(s) - stereochemistry , peptide , chemistry , biochemistry , protein primary structure , peptide sequence , gene
The primary structure of sperm histone H1parecrJinus has been determined. H1 parechinus consists of a polypeptide chain of the following 248 amino acid residues: Pro‐Gly‐Ser‐Pro‐Gln‐Lys‐Arg‐Ala‐Ala‐Ser‐Pro‐Arg‐Lys‐Ser‐Pro‐Arg‐Lys‐Ser‐Pro‐Lys‐Lys‐Ser‐Pro‐Arg‐Lys‐Ala‐Ser‐Ala‐Ser‐Pro‐Arg‐Arg‐Lys‐Ala‐Lys‐Arg‐Ala‐Arg‐Ala‐Ser‐Thr‐His‐Pro‐Pro‐Val‐Leu‐Glu‐Met‐Val‐Gln‐Ala‐Ala‐Ile‐Thr‐Ala‐Met‐Lys‐Glu‐Arg‐Lys‐Gly‐Ser‐Ser‐Ala‐Ala‐Lys‐Ile‐Lys‐Ser‐Tyr‐Met‐Ala‐Ala‐Asn‐Tyr‐Arg‐Val‐Asp‐Met‐Asn‐Val‐Leu‐Ala‐Pro‐His‐Val‐Arg‐Arg‐Ala‐Leu‐Arg‐Asn‐Gly‐Val‐Ala‐Ser‐Gly‐Ala‐Leu‐Lys‐Gln‐Val‐Thr‐Gly‐Thr‐Gly‐Ala‐Ser‐Gly‐Arg‐Phe‐Arg‐Val‐Gly‐Ala‐Val‐Ala‐Lys‐Pro‐Lys‐Lys‐Ala‐Lys‐Lys‐Thr‐Ser‐Ala‐Ala‐Ala‐Lys‐Ala‐Lys‐Lys‐Ala‐Lys‐Ala‐Lys‐Lys‐Lys‐Ala‐Ala‐Ala‐Ala‐Lys‐Arg‐Lys‐Ala‐Ala‐Ala‐Lys‐Ala‐Lys‐Lys‐Ala‐Lys‐Lys‐Pro‐Lys‐Lys‐Lys‐Ala‐Ala‐Lys‐Lys‐Ala‐Lys‐Lys‐Pro‐Ala‐Lys‐Lys‐Ser‐Pro‐Lys‐Lys‐Ala‐Lys‐Lys‐Pro‐Ala‐Lys‐Lys‐Ser‐Pro‐Lys‐Lys‐Lys‐Lys‐Ala‐Lys‐Arg‐Ser‐Pro‐Lys‐Lys‐Ala‐Lys‐Lys‐Ala‐Ala‐G1 y‐Lys‐Arg‐Lys‐Pro‐Ala‐Ala‐Lys‐Lys‐Ala‐Arg‐Arg‐Ser‐Pro‐Arg‐Lys‐Ala‐Gly‐Lys‐Arg‐Arg‐Ser‐Pro‐Lys‐Lys‐Ala‐Arg‐Lys. The protein consists of three domains. Compared to other HI and H5 histones, there is a very similar hydrophobic central domain and the carboxyl‐terminal domain is very rich in lysine and alanine. Hl parechinus is similar to H5 histones in that the carboxyl‐terminal domain also contains many arginine residues close to the carboxyl terminus. The carboxyl‐terminal domain of HI parechinus appears to have been constructed by a series of variable duplications. The amino‐terminal domain of H1 parechinus is longer and quite different to that of other H1 and H5 histones and is characterized by a repeating tetrapeptide of the general type Ser‐Pro‐(basic)2. The known sequence of a histone H1 gene from Psammechinus miliaris [Schaffner, W. et al. (1978) Cell, 14, 655–6711 is compared to the sequence of H1 parechinus . Again the central hydro‐phobic domains are similar whereas the amino terminal domains are very different. The functions of the various domains of sperm histone H1 parechinus are discussed.