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

21 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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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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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.

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SN - 0021-9258

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JF - Journal of Biological Chemistry

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

Abstract

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