Structural basis for interaction between mycobacterium smegmatis Ms6564, a TetR family master regulator, and its target DNA

Shifan Yang; Zengqiang Gao; Tingting Li; Min Yang; Tianyi Zhang; Yuhui Dong; Zheng Guo He

doi:10.1074/jbc.M113.468694

Structural basis for interaction between mycobacterium smegmatis Ms6564, a TetR family master regulator, and its target DNA

Shifan Yang
, Zengqiang Gao
, Tingting Li
, Min Yang
, Tianyi Zhang
, Yuhui Dong
, Zheng Guo He

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Background: The structural basis for interaction between a master regulator and DNA remains unclear. Results: We solved the crystal structures of a broad regulator Ms6564 and its protein-operator complex. Conclusion: Ms6564 binds DNA with strong affinity but makes flexible contacts with DNA. Significance: Ms6564 might slide more easily along the genomic DNA and extensively regulate the expression of diverse genes.

Original language	English
Pages (from-to)	23687-23695
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	288
Issue number	33
DOIs	https://doi.org/10.1074/jbc.M113.468694
State	Published - 16 Aug 2013
Externally published	Yes

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title = "Structural basis for interaction between mycobacterium smegmatis Ms6564, a TetR family master regulator, and its target DNA",

abstract = "Background: The structural basis for interaction between a master regulator and DNA remains unclear. Results: We solved the crystal structures of a broad regulator Ms6564 and its protein-operator complex. Conclusion: Ms6564 binds DNA with strong affinity but makes flexible contacts with DNA. Significance: Ms6564 might slide more easily along the genomic DNA and extensively regulate the expression of diverse genes.",

author = "Shifan Yang and Zengqiang Gao and Tingting Li and Min Yang and Tianyi Zhang and Yuhui Dong and He, \{Zheng Guo\}",

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T1 - Structural basis for interaction between mycobacterium smegmatis Ms6564, a TetR family master regulator, and its target DNA

AU - Yang, Shifan

AU - Gao, Zengqiang

AU - Li, Tingting

AU - Yang, Min

AU - Zhang, Tianyi

AU - Dong, Yuhui

AU - He, Zheng Guo

PY - 2013/8/16

Y1 - 2013/8/16

N2 - Background: The structural basis for interaction between a master regulator and DNA remains unclear. Results: We solved the crystal structures of a broad regulator Ms6564 and its protein-operator complex. Conclusion: Ms6564 binds DNA with strong affinity but makes flexible contacts with DNA. Significance: Ms6564 might slide more easily along the genomic DNA and extensively regulate the expression of diverse genes.

AB - Background: The structural basis for interaction between a master regulator and DNA remains unclear. Results: We solved the crystal structures of a broad regulator Ms6564 and its protein-operator complex. Conclusion: Ms6564 binds DNA with strong affinity but makes flexible contacts with DNA. Significance: Ms6564 might slide more easily along the genomic DNA and extensively regulate the expression of diverse genes.

UR - https://www.scopus.com/pages/publications/84882297330

U2 - 10.1074/jbc.M113.468694

DO - 10.1074/jbc.M113.468694

M3 - Article

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AN - SCOPUS:84882297330

SN - 0021-9258

VL - 288

SP - 23687

EP - 23695

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 33

ER -

Structural basis for interaction between mycobacterium smegmatis Ms6564, a TetR family master regulator, and its target DNA

Abstract

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