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A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria

Authors :
Nicolas Grosjean
Estella F. Yee
Desigan Kumaran
Kriti Chopra
Macon Abernathy
Sandeep Biswas
James Byrnes
Dale F. Kreitler
Jan-Fang Cheng
Agnidipta Ghosh
Steven C. Almo
Masakazu Iwai
Krishna K. Niyogi
Himadri B. Pakrasi
Ritimukta Sarangi
Hubertus van Dam
Lin Yang
Ian K. Blaby
Crysten E. Blaby-Haas
Source :
Nature Communications, Vol 15, Iss 1, Pp 1-18 (2024)
Publication Year :
2024
Publisher :
Nature Portfolio, 2024.

Abstract

Abstract Heme has a critical role in the chemical framework of the cell as an essential protein cofactor and signaling molecule that controls diverse processes and molecular interactions. Using a phylogenomics-based approach and complementary structural techniques, we identify a family of dimeric hemoproteins comprising a domain of unknown function DUF2470. The heme iron is axially coordinated by two zinc-bound histidine residues, forming a distinct two-fold symmetric zinc-histidine-iron-histidine-zinc site. Together with structure-guided in vitro and in vivo experiments, we further demonstrate the existence of a functional link between heme binding by Dri1 (Domain related to iron 1, formerly ssr1698) and post-translational regulation of succinate dehydrogenase in the cyanobacterium Synechocystis, suggesting an iron-dependent regulatory link between photosynthesis and respiration. Given the ubiquity of proteins containing homologous domains and connections to heme metabolism across eukaryotes and prokaryotes, we propose that DRI (Domain Related to Iron; formerly DUF2470) functions at the molecular level as a heme-dependent regulatory domain.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
15
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.9432c18444e92ae265f34950f8b4c
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-024-47486-z