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通过构建新的F'因子对大肠杆菌4.5S RNA中保守碱基的表征

Characterization of conserved bases in 4.5S RNA of Escherichia coli by construction of new F' factors.

作者信息

Peterson James M, Phillips Gregory J

机构信息

Department of Veterinary Microbiology, Iowa State University, 1802 University Boulevard, Building 6, Ames, IA 50011, USA.

出版信息

J Bacteriol. 2008 Dec;190(23):7709-18. doi: 10.1128/JB.00995-08. Epub 2008 Sep 19.

Abstract

To more clearly understand the function of conserved bases of 4.5S RNA, the product of the essential ffs gene of Escherichia coli, and to address conflicting results reported in other studies, we have developed a new genetic system to characterize ffs mutants. Multiple ffs alleles were generated by altering positions that correspond to the region of the RNA molecule that interacts directly with Ffh in assembly of the signal recognition particle. To facilitate characterization of the ffs mutations with minimal manipulation, recombineering was used to construct new F' factors to easily move each allele into different genetic backgrounds for expression in single copy. In combination with plasmids that expressed ffs in multiple copy numbers, the F' factors provided an accurate assessment of the ability of the different 4.5S RNA mutants to function in vivo. Consistent with structural analysis of the signal recognition particle (SRP), highly conserved bases in 4.5S RNA are important for binding Ffh. Despite the high degree of conservation, however, only a single base (C62) was indispensable for RNA function under all conditions tested. To quantify the interaction between 4.5S RNA and Ffh, an assay was developed to measure the ability of mutant 4.5S RNA molecules to copurify with Ffh. Defects in Ffh binding correlated with loss of SRP-dependent protein localization. Real-time quantitative PCR was also used to measure the levels of wild-type and mutant 4.5S RNA expressed in vivo. These results clarify inconsistencies from prior studies and yielded a convenient method to study the function of multiple alleles.

摘要

为了更清楚地了解大肠杆菌必需的ffs基因产物4.5S RNA保守碱基的功能,并解决其他研究中报道的相互矛盾的结果,我们开发了一种新的遗传系统来表征ffs突变体。通过改变与RNA分子中在信号识别颗粒组装过程中直接与Ffh相互作用的区域相对应的位置,产生了多个ffs等位基因。为了在最小操作下便于对ffs突变进行表征,利用重组工程构建新的F'因子,以便轻松地将每个等位基因转移到不同的遗传背景中以单拷贝形式表达。与以多拷贝数表达ffs的质粒相结合,F'因子提供了对不同4.5S RNA突变体在体内发挥功能能力的准确评估。与信号识别颗粒(SRP)的结构分析一致,4.5S RNA中的高度保守碱基对于结合Ffh很重要。然而,尽管保守程度很高,但在所有测试条件下,只有一个碱基(C62)对于RNA功能是不可或缺的。为了量化4.5S RNA与Ffh之间的相互作用,开发了一种测定方法来测量突变型4.5S RNA分子与Ffh共纯化的能力。Ffh结合缺陷与SRP依赖性蛋白质定位丧失相关。实时定量PCR也用于测量体内表达的野生型和突变型4.5S RNA的水平。这些结果澄清了先前研究中的不一致之处,并产生了一种研究多个等位基因功能的便捷方法。

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本文引用的文献

1
Protein translocation across the bacterial cytoplasmic membrane.
Annu Rev Biochem. 2008;77:643-67. doi: 10.1146/annurev.biochem.77.061606.160747.
3
The tmRDB and SRPDB resources.
Nucleic Acids Res. 2006 Jan 1;34(Database issue):D163-8. doi: 10.1093/nar/gkj142.
4
Targeting proteins to membranes: structure of the signal recognition particle.
Curr Opin Struct Biol. 2005 Apr;15(2):213-20. doi: 10.1016/j.sbi.2005.03.007.
5
Simple and highly efficient BAC recombineering using galK selection.
Nucleic Acids Res. 2005 Feb 24;33(4):e36. doi: 10.1093/nar/gni035.
6
SRP-mediated protein targeting: structure and function revisited.
Biochim Biophys Acta. 2004 Nov 11;1694(1-3):17-35. doi: 10.1016/j.bbamcr.2004.03.013.
7
SRP meets the ribosome.
Nat Struct Mol Biol. 2004 Nov;11(11):1049-53. doi: 10.1038/nsmb853.
8
Mechanism of association and reciprocal activation of two GTPases.
PLoS Biol. 2004 Oct;2(10):e320. doi: 10.1371/journal.pbio.0020320. Epub 2004 Sep 21.
9
Structural insights into the signal recognition particle.
Annu Rev Biochem. 2004;73:539-57. doi: 10.1146/annurev.biochem.73.011303.074048.
10

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