Author
Listed:
- Marco Jost
(Massachusetts Institute of Technology)
- Jésus Fernández-Zapata
(Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas)
- María Carmen Polanco
(Area of Genetics (Unidad Asociada al Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas), Faculty of Biology, Universidad de Murcia)
- Juan Manuel Ortiz-Guerrero
(Area of Genetics (Unidad Asociada al Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas), Faculty of Biology, Universidad de Murcia
†Present address: MRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee DD1 5EH, UK.)
- Percival Yang-Ting Chen
(Massachusetts Institute of Technology)
- Gyunghoon Kang
(Massachusetts Institute of Technology)
- S. Padmanabhan
(Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas)
- Montserrat Elías-Arnanz
(Area of Genetics (Unidad Asociada al Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas), Faculty of Biology, Universidad de Murcia)
- Catherine L. Drennan
(Massachusetts Institute of Technology
Massachusetts Institute of Technology
Howard Hughes Medical Institute, Massachusetts Institute of Technology)
Abstract
Photoreceptor proteins enable organisms to sense and respond to light. The newly discovered CarH-type photoreceptors use a vitamin B12 derivative, adenosylcobalamin, as the light-sensing chromophore to mediate light-dependent gene regulation. Here we present crystal structures of Thermus thermophilus CarH in all three relevant states: in the dark, both free and bound to operator DNA, and after light exposure. These structures provide visualizations of how adenosylcobalamin mediates CarH tetramer formation in the dark, how this tetramer binds to the promoter −35 element to repress transcription, and how light exposure leads to a large-scale conformational change that activates transcription. In addition to the remarkable functional repurposing of adenosylcobalamin from an enzyme cofactor to a light sensor, we find that nature also repurposed two independent protein modules in assembling CarH. These results expand the biological role of vitamin B12 and provide fundamental insight into a new mode of light-dependent gene regulation.
Suggested Citation
Marco Jost & Jésus Fernández-Zapata & María Carmen Polanco & Juan Manuel Ortiz-Guerrero & Percival Yang-Ting Chen & Gyunghoon Kang & S. Padmanabhan & Montserrat Elías-Arnanz & Catherine L. Drennan, 2015.
"Structural basis for gene regulation by a B12-dependent photoreceptor,"
Nature, Nature, vol. 526(7574), pages 536-541, October.
Handle:
RePEc:nat:nature:v:526:y:2015:i:7574:d:10.1038_nature14950
DOI: 10.1038/nature14950
Download full text from publisher
As the access to this document is restricted, you may want to search for a different version of it.
Citations
Citations are extracted by the
CitEc Project, subscribe to its
RSS feed for this item.
Cited by:
- Harshwardhan Poddar & Ronald Rios-Santacruz & Derren J. Heyes & Muralidharan Shanmugam & Adam Brookfield & Linus O. Johannissen & Colin W. Levy & Laura N. Jeffreys & Shaowei Zhang & Michiyo Sakuma & J, 2023.
"Redox driven B12-ligand switch drives CarH photoresponse,"
Nature Communications, Nature, vol. 14(1), pages 1-14, December.
- Shaowei Zhang & Laura N. Jeffreys & Harshwardhan Poddar & Yuqi Yu & Chuanyang Liu & Kaylee Patel & Linus O. Johannissen & Lingyun Zhu & Matthew J. Cliff & Cunyu Yan & Giorgio Schirò & Martin Weik & Mi, 2024.
"Photocobilins integrate B12 and bilin photochemistry for enzyme control,"
Nature Communications, Nature, vol. 15(1), pages 1-16, December.
Corrections
All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:526:y:2015:i:7574:d:10.1038_nature14950. See general information about how to correct material in RePEc.
If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.
We have no bibliographic references for this item. You can help adding them by using this form .
If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.
For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .
Please note that corrections may take a couple of weeks to filter through
the various RePEc services.