What determines the folding of the chromatin fiber?
In this review, we attempt to summarize, in a critical manner, what is currently known about the processes of condensation and decondensation of chromatin fibers. We begin with a critical analysis of the possible mechanisms for condensation, considering both old and new evidence as to whether the linker DNA between nucleosomes bends or remains straight in the condensed structure. Concluding that the preponderance of evidence is for straight linkers, we ask what other fundamental process might allow condensation, and argue that there is evidence for linker histone-induced contraction of the internucleosome angle, as salt concentration is raised toward physiological levels. We also ask how certain specific regions of chromatin can become decondensed, even at physiological salt concentration, to allow transcription. We consider linker histone depletion and acetylation of the core histone tails, as possible mechanisms. On the basis of recent evidence, we suggest a unified model linking targeted acetylation of specific genomic regions to linker histone depletion, with unfolding of the condensed fiber as a consequence.
van Holde
K
K
Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331-7305, USA.
Zlatanova
J
J
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D000818:Animals; D002843:Chromatin / Q000648:ultrastructure*; D004247:DNA / Q000648:ultrastructure*; D005786:Gene Expression Regulation; D051548:Histone Acetyltransferases; D006657:Histones / Q000502:physiology*; D046911:Macromolecular Substances; D009707:Nucleosomes / Q000648:ultrastructure*; D009994:Osmolar Concentration; D029701:Saccharomyces cerevisiae Proteins; D055672:Static Electricity; D014158:Transcription, Genetic
D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances; D009707:Nucleosomes; D029701:Saccharomyces cerevisiae Proteins; D004247:DNA; D000123:Acetyltransferases; D051548:Histone Acetyltransferases