A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria
© 2024. The Author(s)..
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.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2024 |
|---|---|
| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:15 |
|---|---|
| Enthalten in: |
Nature communications - 15(2024), 1 vom: 12. Apr., Seite 3167 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Grosjean, Nicolas [VerfasserIn] |
|---|
| Links: |
|---|
| Themen: |
42VZT0U6YR |
|---|
| Anmerkungen: |
Date Completed 15.04.2024 Date Revised 25.04.2024 published: Electronic Citation Status MEDLINE |
|---|
| doi: |
10.1038/s41467-024-47486-z |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM370986784 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM370986784 | ||
| 003 | DE-627 | ||
| 005 | 20240425234118.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 240413s2024 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1038/s41467-024-47486-z |2 doi | |
| 028 | 5 | 2 | |a pubmed24n1386.xml |
| 035 | |a (DE-627)NLM370986784 | ||
| 035 | |a (NLM)38609367 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Grosjean, Nicolas |e verfasserin |4 aut | |
| 245 | 1 | 2 | |a A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria |
| 264 | 1 | |c 2024 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 15.04.2024 | ||
| 500 | |a Date Revised 25.04.2024 | ||
| 500 | |a published: Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2024. The Author(s). | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 7 | |a Heme |2 NLM | |
| 650 | 7 | |a 42VZT0U6YR |2 NLM | |
| 650 | 7 | |a Zinc |2 NLM | |
| 650 | 7 | |a J41CSQ7QDS |2 NLM | |
| 650 | 7 | |a Histidine |2 NLM | |
| 650 | 7 | |a 4QD397987E |2 NLM | |
| 650 | 7 | |a Hemeproteins |2 NLM | |
| 650 | 7 | |a Carbon |2 NLM | |
| 650 | 7 | |a 7440-44-0 |2 NLM | |
| 650 | 7 | |a Iron |2 NLM | |
| 650 | 7 | |a E1UOL152H7 |2 NLM | |
| 700 | 1 | |a Yee, Estella F |e verfasserin |4 aut | |
| 700 | 1 | |a Kumaran, Desigan |e verfasserin |4 aut | |
| 700 | 1 | |a Chopra, Kriti |e verfasserin |4 aut | |
| 700 | 1 | |a Abernathy, Macon |e verfasserin |4 aut | |
| 700 | 1 | |a Biswas, Sandeep |e verfasserin |4 aut | |
| 700 | 1 | |a Byrnes, James |e verfasserin |4 aut | |
| 700 | 1 | |a Kreitler, Dale F |e verfasserin |4 aut | |
| 700 | 1 | |a Cheng, Jan-Fang |e verfasserin |4 aut | |
| 700 | 1 | |a Ghosh, Agnidipta |e verfasserin |4 aut | |
| 700 | 1 | |a Almo, Steven C |e verfasserin |4 aut | |
| 700 | 1 | |a Iwai, Masakazu |e verfasserin |4 aut | |
| 700 | 1 | |a Niyogi, Krishna K |e verfasserin |4 aut | |
| 700 | 1 | |a Pakrasi, Himadri B |e verfasserin |4 aut | |
| 700 | 1 | |a Sarangi, Ritimukta |e verfasserin |4 aut | |
| 700 | 1 | |a van Dam, Hubertus |e verfasserin |4 aut | |
| 700 | 1 | |a Yang, Lin |e verfasserin |4 aut | |
| 700 | 1 | |a Blaby, Ian K |e verfasserin |4 aut | |
| 700 | 1 | |a Blaby-Haas, Crysten E |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Nature communications |d 2010 |g 15(2024), 1 vom: 12. Apr., Seite 3167 |w (DE-627)NLM199274525 |x 2041-1723 |7 nnns |
| 773 | 1 | 8 | |g volume:15 |g year:2024 |g number:1 |g day:12 |g month:04 |g pages:3167 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1038/s41467-024-47486-z |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 15 |j 2024 |e 1 |b 12 |c 04 |h 3167 | ||