CHROMATIN DECONDENSATION

克隆的果蝇核蛋白的Ile结构， 催化脱膜非洲爪蟾精子染色质的去凝聚 （染色质重塑蛋白，CRP 1）在干细胞中进行了研究， 与非洲爪蟾核质蛋白相比， 氨基酸序列 虽然大多数证据表明爪蟾 核质蛋白是五聚体，来自STEM的质量分析表明， CRP I是四聚体（而爪蟾核质蛋白是五聚体）， 与化学交联实验一致。 然而，消极地 染色的CRP I和爪蟾核浆蛋白 在STEM中无法区分。 （Crevel等人，1996年）。 结构 CRP2是第二种热稳定染色质。 重构蛋白 果蝇似乎能够取代突变敲 CRP1目前正在调查中。 超大骨料 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.