Rearrangement of the histone H2A C-terminal domain in the nucleosome.
Using zero-length covalent protein-DNA crosslinking, we have mapped the histone-DNA contacts in nucleosome core particles from which the C- and N-terminal domains of histone H2A were selectively trimmed by trypsin or clostripain. We found that the flexible trypsin-sensitive C-terminal domain of histone H2A contacts the dyad axis, whereas its globular domain contacts the end of DNA in the nucleosome core particle. The appearance of the histone H2A contact at the dyad axis occurs only in the absence of linker DNA and does not depend on the absence of linker histones. Our results show the ability of the histone H2A C-terminal domain to rearrange. This rearrangement might play a biological role in nucleosome disassembly and reassembly and the retention of the H2A-H2B dimer (or the whole octamer) during the passing of polymerases through the nucleosome.
Usachenko
S I
SI
Department of Biological Chemistry, School of Medicine, University of California, Davis 95616.
Bavykin
S G
SG
Gavin
I M
IM
Bradbury
E M
EM
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D003546:Cysteine Endopeptidases / Q000494:pharmacology; D004247:DNA / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000378:metabolism*; D009994:Osmolar Concentration; D011487:Protein Conformation; D014357:Trypsin
D006657:Histones; D009707:Nucleosomes; D004247:DNA; D014357:Trypsin; D003546:Cysteine Endopeptidases; C019913:clostripain