Effect of high mobility group proteins 14 and 17 on the structural and transcriptional properties of acetylated complete and H2A.H2B-deficient nucleosomal cores.
Acetylation of H2A.H2B-deficient nucleosomal cores, like that of the complete particles, causes a substantial increase in the efficiency of the particles as in vitro transcription templates. Binding of the high mobility group proteins 14 and 17 (HMG 14/17) to chemically acetylated nucleosomal particles, both complete nucleosomal cores and those lacking one of the two H2A.H2B dimers, is accompanied by a small structural stabilization. The affinity of HMG 14/17 for the nucleosomal cores is not affected by acetylation of the particles. With acetylated complete and H2A.H2B-deficient cores, the binding of HMG 14/17 does not cause any significant change in the levels of RNA synthesis, which is compatible with the presence of these proteins in transcriptionally active nucleosomes.
Piñeiro
M
M
Centro de Biología Molecular, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
González
P J
PJ
Palacián
E
E
Hernández
F
F
D000107:Acetylation; D000818:Animals; D002645:Chickens; D004912:Erythrocytes; D006609:High Mobility Group Proteins / Q000494:pharmacology*; D006657:Histones / Q000172:deficiency*; D009707:Nucleosomes / Q000737:chemistry / Q000187:drug effects* / Q000378:metabolism; D011489:Protein Denaturation; D014158:Transcription, Genetic / Q000187:drug effects*
D006609:High Mobility Group Proteins; D006657:Histones; D009707:Nucleosomes