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大肠杆菌类核中的结构组织

Architectural organization in E. coli nucleoid.

作者信息

Macvanin Mirjana, Adhya Sankar

机构信息

Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.

出版信息

Biochim Biophys Acta. 2012 Jul;1819(7):830-5. doi: 10.1016/j.bbagrm.2012.02.012. Epub 2012 Feb 22.


DOI:10.1016/j.bbagrm.2012.02.012
PMID:22387214
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7449586/
Abstract

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. coli. 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.

摘要

与真核生物染色体有组织的层次结构不同,细菌染色体被认为没有这样的结构。细菌的基因组被压缩成一种称为类核的紧凑结构。在许多与染色体DNA相关的结构蛋白、类组蛋白中,HU通过弯曲和缠绕DNA将DNA折叠成紧凑结构。与大多数其他类组蛋白不同,HU在真细菌中高度保守,并且具有结合RNA的独特能力。此外,HU突变会深刻改变细胞转录谱,从而对大肠杆菌的生理学和生活方式产生全局性影响。在这里,我们简要概述了类核被组织成不同拓扑结构域的机制。我们提出,HU是产生结构域特异性超螺旋的主要参与者,从而影响组成型启动子的转录谱。本文是名为《时空染色质》特刊的一部分。

相似文献

[1]
Architectural organization in E. coli nucleoid.

Biochim Biophys Acta. 2012-7

[2]
[The bacterial nucleoid].

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[3]
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J Struct Biol. 2006-11

[4]
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[5]
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[6]
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[7]
Coordination of genomic structure and transcription by the main bacterial nucleoid-associated protein HU.

EMBO Rep. 2009-11-13

[8]
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[9]
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[10]
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FEMS Microbiol Lett. 1995-9-15

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Biology (Basel). 2024-12-24

[2]
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[3]
Structure of the E. coli nucleoid-associated protein YejK reveals a novel DNA binding clamp.

Nucleic Acids Res. 2024-7-8

[4]
Stress-induced nucleoid remodeling in Deinococcus radiodurans is associated with major changes in Heat Unstable (HU) protein dynamics.

Nucleic Acids Res. 2024-6-24

[5]
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Nucleic Acids Res. 2024-6-24

[6]
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[7]
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[8]
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[9]
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[10]
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本文引用的文献

[1]
Chromosome organization by a nucleoid-associated protein in live bacteria.

Science. 2011-9-9

[2]
Conversion of commensal Escherichia coli K-12 to an invasive form via expression of a mutant histone-like protein.

mBio. 2011-9-6

[3]
Proteomic analyses of nucleoid-associated proteins in Escherichia coli, Pseudomonas aeruginosa, Bacillus subtilis, and Staphylococcus aureus.

PLoS One. 2011-4-26

[4]
Translation-independent localization of mRNA in E. coli.

Science. 2011-2-25

[5]
Coordination of genomic structure and transcription by the main bacterial nucleoid-associated protein HU.

EMBO Rep. 2009-11-13

[6]
The Chlamydomonas chloroplast HLP protein is required for nucleoid organization and genome maintenance.

Mol Plant. 2009-10-29

[7]
Why and how bacteria localize proteins.

Science. 2009-11-27

[8]
Protein occupancy landscape of a bacterial genome.

Mol Cell. 2009-7-31

[9]
The essential histone-like protein HU plays a major role in Deinococcus radiodurans nucleoid compaction.

Mol Microbiol. 2009-7

[10]
The HU regulon is composed of genes responding to anaerobiosis, acid stress, high osmolarity and SOS induction.

PLoS One. 2009

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