Chromatin core particle obtained by selective cleavage of histones H3 and H4 by clostripain.
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].
Encontre
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C.N.R.S., Faculté de Pharmacie, Montpellier, France.
Parello
J
J
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
D002843:Chromatin; D006657:Histones; D003546:Cysteine Endopeptidases; C019913:clostripain