Modulation of chromatin folding by histone acetylation.
A homogeneous oligonucleosome complex was prepared by reconstitution of highly hyperacetylated histone octamers onto a linear DNA template consisting of 12 tandemly arranged 208-base pair fragments of the 5 S rRNA gene from the sea urchin Lytechinus variegatus. The ionic strength-dependent folding of this oligonucleosome assembly was monitored by sedimentation velocity and electron microscopy. Both types of analysis indicate that under ionic conditions resembling those found in the physiological range and in the absence of histone H1, the acetylated oligonucleosome complexes remain in an extended conformation in contrast to their nonacetylated counterparts. The implications of this finding in the context of a multistate model of chromatin folding (Hansen, J. C., and Ausio, J. (1992) TIBS 197, 187-191) as well as its biological relevance are discussed.
Garcia-Ramirez
M
M
Institut de Recerca Oncologica, Hospital Duran Reynals, Barcelona, Spain.
Rocchini
C
C
Ausio
J
J
D000107:Acetylation; D000818:Animals; D002645:Chickens; D002843:Chromatin / Q000378:metabolism* / Q000648:ultrastructure; D004247:DNA / Q000737:chemistry; D006367:HeLa Cells; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008854:Microscopy, Electron; D009690:Nucleic Acid Conformation; D009994:Osmolar Concentration; D017510:Protein Folding; D012617:Sea Urchins; D013698:Templates, Genetic
D002843:Chromatin; D006657:Histones; D004247:DNA