HMG proteins 14 and 17 become cross-linked to the globular domain of histone H3 near the nucleosome core particle dyad.
HMG proteins were derivatized with the photoactivatable cross-linker N-succinimidyl 3-((4-azidophenyl)dithio)propionate and then allowed to associate with nucleosome core particles. Following photolysis, peptide mapping of the principal dimeric adducts was carried out. Cross-linking occurred primarily from a central location in the HMGs to a central location in H3. The positions of these cross-links, considered along with other data from the literature, show that HMG proteins 14 and 17 make important contacts to H3 near the front face of the nucleosome. This raises the possibility that HMGs 14 and 17 participate in the reported conformational transition which exposes the H3 sulfhydryls of active nucleosomes.
Brawley
J V
JV
Department of Chemistry and Biochemistry, University of California, Los Angeles 90024.
Martinson
H G
HG
D000818:Animals; D001386:Azides / Q000737:chemistry; D002645:Chickens; D003432:Cross-Linking Reagents; D006609:High Mobility Group Proteins / Q000737:chemistry*; D006657:Histones / Q000737:chemistry*; D009707:Nucleosomes / Q000737:chemistry*; D010449:Peptide Mapping; D010782:Photolysis; D011487:Protein Conformation
D001386:Azides; D003432:Cross-Linking Reagents; D006609:High Mobility Group Proteins; D006657:Histones; D009707:Nucleosomes; C033169:3-((4-azidophenyl)dithio)propionic N-hydroxysuccinimide