Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression.
Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression.
复制标题
HMG1 和接头组蛋白 B4 和 H1 与双核小体 DNA 的差异关联:结构转变和转录抑制。
作者:
Kiyoe Ura;Karl Nightingale;Alan P. Wolffe
We examined the structural and functional consequences of incorporating either histone H1, histone B4 or HMG1 into a synthetic dinucleosome containing two 5S rRNA genes. We found that all three proteins bind to linker DNA, stabilizing an additional 20 bp from micrococcal nuclease digestion and restrict nucleosome mobility. Histone H1 has the highest‐affinity interaction with the dinucleosome; histone B4 and HMG1 associate with significantly reduced affinities. We found that histone H1 binds to the dinucleosome template with a dissociation constant (KD) of 7.4 nM, whereas the KD is 45 nM for histone B4 and 300 nM for HMG1. The KDs for the interaction of these proteins with naked DNA are 18 nM for H1, 80 nM for B4 and 300 nM for HMG1. The differences in association of these proteins with the dinucleosome are reflected in the efficiency with which the different proteins repress transcription from the 5S rRNA genes. Thus, although all three proteins can contribute to the organization of chromatin, the stability of the structures they assemble will vary. Our results provide a molecular explanation for the transcriptional promiscuity of Xenopus early embryonic chromatin, which is enriched in HMG1 and linker histone B4, but deficient in histone H1.
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影响因子:
10.5
作者:
PAULL, TT;HAYKINSON, MJ;JOHNSON, RC
通讯作者:
JOHNSON, RC
DOI:
10.1073/pnas.91.9.3525
发表时间:
1994
影响因子:
11.1
作者:
Varga-Weisz,P;Zlatanova,J;Leuba,SH;Schroth,GP;vanHolde,K
通讯作者:
vanHolde,K
影响因子:
10.5
作者:
SHYKIND, BM;KIM, J;SHARP, PA
通讯作者:
SHARP, PA
影响因子:
2.9
作者:
Jackson,JB;Rill,RL
通讯作者:
Rill,RL