Spassky A, Rimsky S, Garreau H, Buc H
Nucleic Acids Res. 1984 Jul 11;12(13):5321-40. doi: 10.1093/nar/12.13.5321.
We characterize a component of the E. coli bacterial nucleoid H1a, which accumulates in stationary phase. This protein, identical with the major component of a plasmid-protein complex previously isolated in our laboratory, has a pI close to 7.5. Acrylamide gel electrophoresis and sedimentation in sucrose gradient have shown that the protein H1a induces significant compaction into DNA. This compaction is equivalent to that observed in nucleosome core although it introduces only a slight change in linking number. In addition, the structural change induced in the lactose L8UV5 promoter by H1a results in the decrease in the kinetic of formation of the open complex with RNA polymerase.
我们对大肠杆菌类核H1a的一个组分进行了表征，该组分在稳定期积累。这种蛋白质与我们实验室先前分离的质粒 - 蛋白质复合物的主要成分相同，其等电点接近7.5。丙烯酰胺凝胶电泳和蔗糖梯度沉降表明，蛋白质H1a可使DNA发生显著压缩。这种压缩与在核小体核心中观察到的压缩相当，尽管它仅使连接数发生轻微变化。此外，H1a在乳糖L8UV5启动子中诱导的结构变化导致与RNA聚合酶形成开放复合物的动力学降低。
