Immunochemical analysis of the exposure of high mobility group protein 14 and 17 surfaces in chromatin.
Antisera were elicited against synthetic peptides corresponding either to regions common to all members of the high mobility group 14 and 17 protein family protein or to distinct domains of the HMG-14 or HMG-17 subgroup. The antisera were used to probe the accessibility of various HMG domains in chromatin. Competitive enzyme-linked immunosorbent assays indicate that the central region of the proteins, which contains their DNA binding domain and is positively charged, is exposed to a smaller degree than the C-terminal region of the proteins, which has a net negative charge. The C-terminal regions of the HMG-14 and HMG-17 proteins are exposed and available to interact with other proteins.
Bustin
M
M
Laboratory of Molecular Carcinogenesis, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.
Crippa
M P
MP
Pash
J M
JM
D000595:Amino Acid Sequence; D000818:Animals; D000936:Antigen-Antibody Complex; D001667:Binding, Competitive; D002467:Cell Nucleus / Q000648:ultrastructure; D002645:Chickens; D002843:Chromatin / Q000737:chemistry / Q000648:ultrastructure*; D004797:Enzyme-Linked Immunosorbent Assay; D004912:Erythrocytes / Q000737:chemistry; D006367:HeLa Cells / Q000737:chemistry; D006609:High Mobility Group Proteins / Q000032:analysis* / Q000276:immunology / Q000648:ultrastructure; D006657:Histones / Q000648:ultrastructure; D006801:Humans; D007106:Immune Sera; D008961:Models, Structural; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000648:ultrastructure; D010455:Peptides / Q000138:chemical synthesis; D011487:Protein Conformation
D000936:Antigen-Antibody Complex; D002843:Chromatin; D006609:High Mobility Group Proteins; D006657:Histones; D007106:Immune Sera; D009707:Nucleosomes; D010455:Peptides