title: Chromatin core particle obtained by selective cleavage of histones H3 and H4 by clostripain.
abstract: A new chromatin core particle characterized by a half-proteolyzed octamer is obtained by controlled digestion of the native core particle by clostripain. The proteolyzed histones correspond to four polypeptide fragments which are tentatively assigned to H2A[4-129], H2B[1-125], H3[27-135] and H4[18-102] on the basis of electrophoretic evidence and the known specificity of clostripain for arginyl residues. Despite the loss of the N-terminal regions of histones H3 and H4, the partially proteolyzed core particle retains the structural conformation of the native one as shown by circular dichroism. As expected, this half-proteolyzed core particle presents an intermediate accessibility to polycations, such as spermidine, in comparison with that observed with the native core particle and a fully proteolyzed core particle. The latter includes the polypeptide fragments H2A[12-129], H2B[21-125], H3[27-135] and H4[20-102].
authors.affiliation: C.N.R.S., Faculté de Pharmacie, Montpellier, France.
authors.forename: I
authors.initials: I
authors.lastname: Encontre
authors.forename: J
authors.initials: J
authors.lastname: Parello
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002843:Chromatin / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism*; D051381:Rats
chemical_list: D002843:Chromatin; D006657:Histones; D003546:Cysteine Endopeptidases; C019913:clostripain