Architectural organization in E. coli nucleoid

被引:62
|
作者
Macvanin, Mirjana [1 ]
Adhya, Sankar [1 ]
机构
[1] NCI, Mol Biol Lab, Ctr Canc Res, NIH, Bethesda, MD 20892 USA
基金
美国国家卫生研究院;
关键词
Nucleoid; Histone-like protein; HU; Chromosome organization; HISTONE-LIKE PROTEIN; DNA-BINDING PROTEIN; LACKING HU PROTEIN; HOST FACTOR IHF; ESCHERICHIA-COLI; BACTERIAL GENOME; ELECTRON-MICROSCOPY; FOLDED CHROMOSOMES; GENE-REGULATION; CELL-DIVISION;
D O I
10.1016/j.bbagrm.2012.02.012
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In contrast to organized hierarchical structure of eukaryotic chromosome, bacterial chromosomes are believed not to have such structures. The genomes of bacteria are condensed into a compact structure called the nucleoid. Among many architectural, histone-like proteins which associate with the chromosomal DNA is HU which is implicated in folding DNA into a compact structure by bending and wrapping DNA. Unlike the majority of other histone-like proteins. HU is highly conserved in eubacteria and unique in its ability to bind RNA. Furthermore, an HU mutation profoundly alters the cellular transcription profile and consequently has global effects on physiology and the lifestyle of E. colt. Here we provide a short overview of the mechanisms by which the nucleoid is organized into different topological domains. We propose that HU is a major player in creating domain-specific superhelicities and thus influences the transcription profile from the constituent promoters. This article is part of a Special Issue entitled: Chromatin in time and space. Published by Elsevier B.V.
引用
收藏
页码:830 / 835
页数:6
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