Redox-dependent ligand switching in a sensory heme-binding GAF domain of the cyanobacterium nostoc sp. PCC7120

Kun Tang; Markus Knipp; Bing Bing Liu; Nicholas Cox; Robert Stabel; Qi He; Ming Zhou; Hugo Scheer; Kai Hong Zhao; Wolfgang Gärtner

doi:10.1074/jbc.M115.654087

Redox-dependent ligand switching in a sensory heme-binding GAF domain of the cyanobacterium nostoc sp. PCC7120

Kun Tang, Markus Knipp, Bing Bing Liu, Nicholas Cox, Robert Stabel, Qi He, Ming Zhou, Hugo Scheer, Kai Hong Zhao, Wolfgang Gärtner^*

^*Corresponding author for this work

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

11 Citations (Scopus)

Abstract

Background: Three GAF domain proteins from cyanobacteria (Nostoc PCC7120) identified with heme group binding signatures. Results: Protein All4978 composed of a heme-binding domain and a helix-turn-helix (HtH) motif switches ligands from cysteine (ferric state) to histidine (ferrous state) and binds DNA preferentially in ferric state. Conclusion: The ligand-switch mechanism suggests redox-dependent signaling. Significance: HtH activity regulation by a GAF-bound heme is novel for cyanobacteria.

Original language	English
Pages (from-to)	19067-19080
Number of pages	14
Journal	Journal of Biological Chemistry
Volume	290
Issue number	31
DOIs	https://doi.org/10.1074/jbc.M115.654087
Publication status	Published - 31 Jul 2015
Externally published	Yes

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@article{b8aaf9ae136b4e0591adf377eb46535a,

title = "Redox-dependent ligand switching in a sensory heme-binding GAF domain of the cyanobacterium nostoc sp. PCC7120",

abstract = "Background: Three GAF domain proteins from cyanobacteria (Nostoc PCC7120) identified with heme group binding signatures. Results: Protein All4978 composed of a heme-binding domain and a helix-turn-helix (HtH) motif switches ligands from cysteine (ferric state) to histidine (ferrous state) and binds DNA preferentially in ferric state. Conclusion: The ligand-switch mechanism suggests redox-dependent signaling. Significance: HtH activity regulation by a GAF-bound heme is novel for cyanobacteria.",

author = "Kun Tang and Markus Knipp and Liu, \{Bing Bing\} and Nicholas Cox and Robert Stabel and Qi He and Ming Zhou and Hugo Scheer and Zhao, \{Kai Hong\} and Wolfgang G{\"a}rtner",

note = "Publisher Copyright: {\textcopyright} 2015 by The American Society for Biochemistry and Molecular Biology, Inc.",

year = "2015",

month = jul,

day = "31",

doi = "10.1074/jbc.M115.654087",

language = "English",

volume = "290",

pages = "19067--19080",

journal = "Journal of Biological Chemistry",

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TY - JOUR

T1 - Redox-dependent ligand switching in a sensory heme-binding GAF domain of the cyanobacterium nostoc sp. PCC7120

AU - Tang, Kun

AU - Knipp, Markus

AU - Liu, Bing Bing

AU - Cox, Nicholas

AU - Stabel, Robert

AU - He, Qi

AU - Zhou, Ming

AU - Scheer, Hugo

AU - Zhao, Kai Hong

AU - Gärtner, Wolfgang

PY - 2015/7/31

Y1 - 2015/7/31

N2 - Background: Three GAF domain proteins from cyanobacteria (Nostoc PCC7120) identified with heme group binding signatures. Results: Protein All4978 composed of a heme-binding domain and a helix-turn-helix (HtH) motif switches ligands from cysteine (ferric state) to histidine (ferrous state) and binds DNA preferentially in ferric state. Conclusion: The ligand-switch mechanism suggests redox-dependent signaling. Significance: HtH activity regulation by a GAF-bound heme is novel for cyanobacteria.

AB - Background: Three GAF domain proteins from cyanobacteria (Nostoc PCC7120) identified with heme group binding signatures. Results: Protein All4978 composed of a heme-binding domain and a helix-turn-helix (HtH) motif switches ligands from cysteine (ferric state) to histidine (ferrous state) and binds DNA preferentially in ferric state. Conclusion: The ligand-switch mechanism suggests redox-dependent signaling. Significance: HtH activity regulation by a GAF-bound heme is novel for cyanobacteria.

UR - https://www.scopus.com/pages/publications/84940561655

U2 - 10.1074/jbc.M115.654087

DO - 10.1074/jbc.M115.654087

M3 - Article

SN - 0021-9258

VL - 290

SP - 19067

EP - 19080

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 31

ER -

Redox-dependent ligand switching in a sensory heme-binding GAF domain of the cyanobacterium nostoc sp. PCC7120

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