Horn P J, Peterson C L
University of Massachusetts Medical School, Program in Molecular Medicine, 373 Plantation St., Worcester, MA 01605, USA.
Front Biosci. 2001 Aug 1;6:D1019-23. doi: 10.2741/horn.
In eukaryotes, processes requiring access to DNA are inhibited by the structural packaging of the genome. A number of specialized ATP-dependent chromatin remodeling enzymes have evolved to overcome this inhibition. One subset of these enzymes, SWI/SNF, plays a critical role in the regulation of transcription, often functioning in concert with nuclear histone acetyltransferases (HATs). It remains unknown how these activities are coordinated. However, recent results revealing that the bromodomain, a motif common in these remodeling factors, constitutes an acetyl-lysine binding domain might provide insight into this process. Bromodomains may serve a role analogous to the signal transduction SH2 domain, by providing a means to recruit remodeling complexes to acetylated chromatin regions or to allosterically modify their function post-recruitment.
在真核生物中，需要接触DNA的过程会受到基因组结构包装的抑制。已经进化出许多专门的依赖ATP的染色质重塑酶来克服这种抑制。这些酶的一个子集，即SWI/SNF，在转录调控中起关键作用，通常与核组蛋白乙酰转移酶（HATs）协同发挥作用。这些活性如何协调仍不清楚。然而，最近的结果表明，这些重塑因子中常见的基序——溴结构域，构成了一个乙酰赖氨酸结合结构域，这可能为深入了解这一过程提供线索。溴结构域可能起到类似于信号转导SH2结构域的作用，通过提供一种将重塑复合物招募到乙酰化染色质区域的方式，或在招募后对其功能进行变构修饰。
