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Nap1与组蛋白相互作用的热力学模型。

A thermodynamic model for Nap1-histone interactions.

作者信息

Andrews Andrew J, Downing Gregory, Brown Kitty, Park Young-Jun, Luger Karolin

机构信息

Howard Hughes Medical Institute and Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870, USA.

出版信息

J Biol Chem. 2008 Nov 21;283(47):32412-8. doi: 10.1074/jbc.M805918200. Epub 2008 Aug 25.

DOI:10.1074/jbc.M805918200
PMID:18728017
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2583301/
Abstract

The yeast nucleosome assembly protein 1 (yNap1) plays a role in chromatin maintenance by facilitating histone exchange as well as nucleosome assembly and disassembly. It has been suggested that yNap1 carries out these functions by regulating the concentration of free histones. Therefore, a quantitative understanding of yNap1-histone interactions also provides information on the thermodynamics of chromatin. We have developed quantitative methods to study the affinity of yNap1 for histones. We show that yNap1 binds H2A/H2B and H3/H4 histone complexes with low nm affinity, and that each yNap1 dimer binds two histone fold dimers. The yNap1 tails contribute synergistically to histone binding while the histone tails have a slightly repressive effect on binding. The (H3/H4)(2) tetramer binds DNA with higher affinity than it binds yNap1.

摘要

酵母核小体组装蛋白1（yNap1）通过促进组蛋白交换以及核小体的组装和拆卸，在染色质维持中发挥作用。有人提出，yNap1通过调节游离组蛋白的浓度来执行这些功能。因此，对yNap1与组蛋白相互作用的定量理解也提供了有关染色质热力学的信息。我们已经开发出定量方法来研究yNap1对组蛋白的亲和力。我们发现yNap1以低纳米亲和力结合H2A/H2B和H3/H4组蛋白复合物，并且每个yNap1二聚体结合两个组蛋白折叠二聚体。yNap1的尾部对组蛋白结合有协同作用，而组蛋白的尾部对结合有轻微的抑制作用。（H3/H4）2四聚体与DNA的结合亲和力高于与yNap1的结合亲和力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/179dc9119e48/zbc0460854490005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/dd3f7c347b8f/zbc0460854490001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/cc27d0023ec7/zbc0460854490002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/c15ec86d252d/zbc0460854490003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/e0186d114f37/zbc0460854490004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/179dc9119e48/zbc0460854490005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/dd3f7c347b8f/zbc0460854490001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/cc27d0023ec7/zbc0460854490002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/c15ec86d252d/zbc0460854490003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/e0186d114f37/zbc0460854490004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bd6/2583301/179dc9119e48/zbc0460854490005.jpg

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2
A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1.包含核定位序列的β-发夹结构维持核小体组装蛋白1的自缔合状态。
J Mol Biol. 2008 Jan 25;375(4):1076-85. doi: 10.1016/j.jmb.2007.11.031. Epub 2007 Nov 19.
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