The loss of one H2A.H2B dimer from the nucleosomal core increases its affinity for RNA polymerase II and its efficiency as a transcription template, allowing transcription of the entire DNA present in the particle. In contrast, the nucleosomal core lacking the amino-terminal ends of histones, which has an affinity for polymerase equal to that of the H2A.H2B-deficient core, shows transcription properties similar to those of the whole nucleosomal core, with synthesis of short RNA chains (40 nucleotides or less). Similar results were obtained with a bacterial RNA polymerase. The improved efficiency of the H2A.H2B-deficient cores as transcription templates does not appear to be produced by nonspecific loss of protein or structural relaxation of the particle. These results suggest that a particle lacking one H2A.H2B dimer might be a necessary intermediate during in vivo transcription.
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