Differential ligand-selective control of opposing enzymatic activities within a bifunctional c-di-GMP enzyme
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- Dayna C. Patterson
- Department of Chemistry, The Pennsylvania State University, University Park, PA 16802;
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- Myrrh Perez Ruiz
- Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802;
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- Hyerin Yoon
- Department of Chemistry, Emory University, Atlanta, GA 30322;
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- Johnnie A. Walker
- Department of Chemistry, Emory University, Atlanta, GA 30322;
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- Jean-Paul Armache
- Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802;
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- Neela H. Yennawar
- The Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, PA 16802
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- Emily E. Weinert
- Department of Chemistry, The Pennsylvania State University, University Park, PA 16802;
書誌事項
- 公開日
- 2021-09-02
- 権利情報
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- https://www.pnas.org/site/aboutpnas/licenses.xhtml
- DOI
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- 10.1073/pnas.2100657118
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:title>Significance</jats:title><jats:p>Bifunctional enzymes are widely distributed throughout bacteria and are involved in modulating bacterial phenotypes; however, regulatory mechanisms that control the activities of the opposing output domains have remained elusive. Studies on DcpG demonstrate that binding of ligands to the sensor globin domain differentially affect GGDEF and EAL domain activities and highlight a role for protein conformational changes in modulating enzymatic activity. Unusual sensor globin domain characteristics, including heme midpoint potentials, are likely important for the unique regulatory properties of DcpG. As<jats:italic>Paenibacillus dendritiformis</jats:italic>responds to changes in the gaseous environment by modulating biofilm formation, DcpG is likely important in modulating physiological responses to changes in O<jats:sub>2</jats:sub>and NO levels, identifying a role for heme sensor signaling in the bacterium.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 118 (36), 2021-09-02
Proceedings of the National Academy of Sciences