CHROMATIN DECONDENSATION

克隆的果蝇核蛋白的Ile结构 催化去膜非洲爪哇精子染色质的解缩 (染色质重塑蛋白，CRP1)在STEM中被研究以 将其与非洲爪哇核纤溶酶进行比较，发现它在 氨基酸序列。虽然大多数证据表明非洲爪哇 核纤溶酶是五聚体，来自STEM的质量分析表明 CRP I是四聚体(而非洲爪哇核纤溶酶是五聚体)，在 与化学交联剂实验结果一致。然而，负面的 染色的C反应蛋白I和非洲爪哇核纤溶酶的形态 在STEM中难以区分。(Crevel等人，1996)。该结构 CRP2的第二个热稳定染色质。血管重塑蛋白 一种果蝇，似乎能够代替突变的敲门声 C反应蛋白1，目前正在调查中。非常大的集合体 已经被观察到了。

Ile structure of a cloned Drosophila nuclear protein which can catalyze the decondensation of demembranated Xenopus sperm chromatin (chromatin remodeling protein, CRP 1) was studied in the STEM to compare it to Xenopus nucleoplasmin to which it is quite homologous in amino acid sequence. While most evidence suggests that Xenopus nucleoplasmin is pentameric, mass analysis from the STEM suggests that CRP I is tetrameric (while Xenopus nucleoplasmin is pentameric), in agreement with chemical crosslinking experiments. However, negatively stained CRP I and Xenopus nucleoplasmin were morphologically indistinguishable in the STEM. (Crevel et al., 1996). The structure of CRP2, a second heat-stable chromatin. remodeling protein of Drosophild which appears to be able to substitute in a mutant knocking out CRP 1, is currently under investigation. Very large aggregates have been observed.