Change in the pattern of histone binding to DNA upon transcriptional activation.
Patterns of histone binding to DNA of transcriptionally active D. melanogaster hsp70 genes within the nuclei have been analyzed by two methods of histone-DNA chemical cross-linking. When cross-linking is restricted to the central, "globular" regions of histones, it drops most for H1, to an intermediate extent for H2A and H2B, and least for H3 and H4 in transcriptionally active versus transcriptionally silent chromatin. When it occurs via histone terminal regions as well, cross-linking is quantitatively similar for active and inactive chromatin. Neither cross-linking method detects histones on the hsp70 promoter region. It appears that chromatin activation decreases histone binding to DNA via the "globular" regions, known to be essential for the folding of nucleosomes and the 30 nm chromatin fibril, but does not significantly affect the interaction of flexible and loosely bound histone "tails" with DNA. The role of these histone-DNA interaction changes in the unfolding of active chromatin and RNA polymerase reading through histone-bound DNA is discussed.
Nacheva
G A
GA
W. A. Engelhardt Institute of Molecular Biology, Academy of Sciences of the USSR, Moscow.
Guschin
D Y
DY
Preobrazhenskaya
O V
OV
Karpov
V L
VL
Ebralidse
K K
KK
Mirzabekov
A D
AD
D000818:Animals; D003432:Cross-Linking Reagents; D004247:DNA / Q000378:metabolism*; D004331:Drosophila melanogaster; D006360:Heat-Shock Proteins / Q000235:genetics; D006639:Histidine; D006657:Histones / Q000378:metabolism*; D008239:Lysine; D009707:Nucleosomes / Q000648:ultrastructure*; D014158:Transcription, Genetic
D003432:Cross-Linking Reagents; D006360:Heat-Shock Proteins; D006657:Histones; D009707:Nucleosomes; D006639:Histidine; D004247:DNA; D008239:Lysine