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Intracytoplasmic-membrane development in alphaproteobacteria involves the homolog of the mitochondrial crista-developing protein Mic60
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SYSNO ASEP 0572376 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Intracytoplasmic-membrane development in alphaproteobacteria involves the homolog of the mitochondrial crista-developing protein Mic60 Author(s) Munoz-Gomez, S.A. (US)
Cadena, Lawrence Rudy (BC-A) RID, ORCID
Gardiner, Alastair T. (MBU-M) ORCID
Leger, M.M. (ES)
Sheikh, Shaghayegh (BC-A) ORCID
Connell, L.B. (CA)
Bílý, Tomáš (BC-A) ORCID
Kopejtka, Karel (MBU-M) ORCID, RID
Beatty, J.T. (CA)
Koblížek, Michal (MBU-M) RID, ORCID
Roger, A.J. (CA)
Slamovits, C.H. (CA)
Lukeš, Julius (BC-A) RID, ORCID
Hashimi, Hassan (BC-A) RID, ORCIDNumber of authors 14 Source Title Current Biology. - : Cell Press - ISSN 0960-9822
Roč. 33, č. 6 (2023), s. 1099-+Number of pages 31 s. Publication form Print - P Language eng - English Country US - United States Keywords Intracytoplasmic-membrane ; mitochondrial ; crista-developing protein Mic60 Subject RIV EE - Microbiology, Virology OECD category Microbiology Subject RIV - cooperation Institute of Microbiology - Microbiology, Virology R&D Projects GA20-23513S GA ČR - Czech Science Foundation (CSF) GX19-28778X GA ČR - Czech Science Foundation (CSF) EF16_019/0000759 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LM2015062 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Limited access Institutional support BC-A - RVO:60077344 ; MBU-M - RVO:61388971 UT WOS 000969910700001 EID SCOPUS 85150373308 DOI https://doi.org/10.1016/j.cub.2023.02.059 Annotation Mitochondrial cristae expand the surface area of respiratory membranes and ultimately allow for the evolutionary scaling of respiration with cell volume across eukaryotes. The discovery of Mic60 homologs among alphaproteobacteria, the closest extant relatives of mitochondria, suggested that cristae might have evolved from bacterial intracytoplasmic membranes (ICMs). Here, we investigated the predicted structure and function of alphaproteobacterial Mic60, and a protein encoded by an adjacent gene Orf52, in two distantly related purple alphaproteobacteria, Rhodobacter sphaeroides and Rhodopseudo-monas palustris. In addition, we assessed the potential physical interactors of Mic60 and Orf52 in R. sphaeroides. We show that the three a helices of mitochondrial Mic60's mitofilin domain, as well as its adjacent membrane-binding amphipathic helix, are present in alphaproteobacterial Mic60. The disrup-tion of Mic60 and Orf52 caused photoheterotrophic growth defects, which are most severe under low light conditions, and both their disruption and overexpression led to enlarged ICMs in both studied alphapro-teobacteria. We also found that alphaproteobacterial Mic60 physically interacts with BamA, the homolog of Sam50, one of the main physical interactors of eukaryotic Mic60. This interaction, responsible for mak-ing contact sites at mitochondrial envelopes, has been conserved in modern alphaproteobacteria despite more than a billion years of evolutionary divergence. Our results suggest a role for Mic60 in photosynthetic ICM development and contact site formation at alphaproteobacterial envelopes. Overall, we provide sup-port for the hypothesis that mitochondrial cristae evolved from alphaproteobacterial ICMs and have there-fore improved our understanding of the nature of the mitochondrial ancestor. Workplace Biology Centre (since 2006) Contact Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Year of Publishing 2024 Electronic address https://www.sciencedirect.com/science/article/abs/pii/S0960982223001999?via%3Dihub
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