Genetic Analysis of Phage Mu Mor Protein Amino Acids Involved in DNA Minor Groove Binding and Conformational Changes

被引：1

作者：

Kumaraswami, Muthiah ^{[1
]}

Avanigadda, Lakshmi ^{[1
]}

Rai, Rajendra ^{[1
]}

Park, Hee-Won ^{[2
]}

Howe, Martha M. ^{[1
]}

机构：

[1] Univ Tennessee, Hlth Sci Ctr, Dept Microbiol Immunol & Biochem, Memphis, TN 38163 USA

[2] Univ Toronto, Dept Pharmacol, Struct Genom Consortium, Toronto, ON M5G 1L7, Canada

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2011年 / 286卷 / 41期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

OPERATOR COMPLEX REVEALS; BACTERIOPHAGE-MU; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; GENOME SEQUENCE; TRANSCRIPTION ACTIVATION; POSITIVE REGULATOR; TERMINAL DOMAIN; RNA-POLYMERASE; P-M;

D O I：

10.1074/jbc.M111.269860

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：

Background: The phage Mu Mor activator protein structure led to predictions of key amino acids needed for DNA binding. Results: Mutational analysis identified specific Mor amino acids needed for DNA binding and transcription activation. Conclusion: The properties of the mutants support the predictions from the structure. Significance: The Mor protein family is unique among regulatory proteins.

引用

页码：35852 / 35862

页数：11

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