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一种核蛋白修饰酶对有序染色质结构有反应。

A nuclear protein-modifying enzyme is responsive to ordered chromatin structure.

作者信息

Butt T R, Brothers J F, Giri C P, Smulson M E

出版信息

Nucleic Acids Res. 1978 Aug;5(8):2775-88. doi: 10.1093/nar/5.8.2775.

Abstract

Poly (ADP-ribose) polymerase, a nuclear protein-modifying enzyme, binds to the internucleosomal linker region of chromatin, although it modifies certain core nucleosomal histones in addition to histone H1. The activity per unit of DNA chromatin changes with the nucleosome repeat number. It reaches a maximum on chromatin of 8-10 nucleosomes in length. As the complexity of chromatin with respect to nucleosome repeat number and compactness increases, a decline and stabilization of specific activity is noted. The difference in specific activity is maintained through resedimentation and dialysis of particles. It does not appear due to differences in polymer chain length or differential degradation of poly (ADP-ribose). The data suggest a relationship between ADP-ribosylation and chromatin organization and vice versa.

摘要

聚(ADP-核糖)聚合酶是一种核蛋白修饰酶,它结合于染色质的核小体间连接区,不过除了组蛋白H1之外,它还修饰某些核心核小体组蛋白。每单位DNA染色质的活性会随着核小体重复数而变化。在长度为8至10个核小体的染色质上它达到最大值。随着染色质在核小体重复数和紧密程度方面的复杂性增加,会观察到比活性的下降和稳定。通过颗粒的再沉降和透析可维持比活性的差异。它并非由于聚合物链长度的差异或聚(ADP-核糖)的差异降解而出现。这些数据表明ADP-核糖基化与染色质组织之间存在关联,反之亦然。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/67bb/342206/24fe962843c3/nar00469-0093-a.jpg

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