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Structure of transcription factor HetR required for heterocyst differentiation in cyanobacteria.


ABSTRACT: HetR is an essential regulator of heterocyst development in cyanobacteria. HetR binds to a DNA palindrome upstream of the hetP gene. We report the crystal structure of HetR from Fischerella at 3.0 ?. The protein is a dimer comprised of a central DNA-binding unit containing the N-terminal regions of the two subunits organized with two helix-turn-helix motifs; two globular flaps extending in opposite directions; and a hood over the central core formed from the C-terminal subdomains. The flaps and hood have no structural precedent in the protein database, therefore representing new folds. The structural assignments are supported by site-directed mutagenesis and DNA-binding studies. We suggest that HetR serves as a scaffold for assembly of transcription components critical for heterocyst development.

SUBMITTER: Kim Y 

PROVIDER: S-EPMC3121805 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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Structure of transcription factor HetR required for heterocyst differentiation in cyanobacteria.

Kim Youngchang Y   Joachimiak Grazyna G   Ye Zi Z   Binkowski T Andrew TA   Zhang Rongguang R   Gornicki Piotr P   Callahan Sean M SM   Hess Wolfgang R WR   Haselkorn Robert R   Joachimiak Andrzej A  

Proceedings of the National Academy of Sciences of the United States of America 20110531 25


HetR is an essential regulator of heterocyst development in cyanobacteria. HetR binds to a DNA palindrome upstream of the hetP gene. We report the crystal structure of HetR from Fischerella at 3.0 Å. The protein is a dimer comprised of a central DNA-binding unit containing the N-terminal regions of the two subunits organized with two helix-turn-helix motifs; two globular flaps extending in opposite directions; and a hood over the central core formed from the C-terminal subdomains. The flaps and  ...[more]

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