Biochimica et Biophysica Acta-Bioenergetics最新文献_第2页

New insights into the involvement of residue D1/V185 in photosystem II function in Synechocystis 6803 and Thermosynechococcus vestitus 残基D1/V185参与6803聚囊球菌和残余热聚球菌光系统II功能的新认识

IF 3.4 2区生物学

Biochimica et Biophysica Acta-Bioenergetics Pub Date : 2025-02-25 DOI: 10.1016/j.bbabio.2025.149550

Alain Boussac , Julien Sellés , Miwa Sugiura , Robert L. Burnap

{"title":"New insights into the involvement of residue D1/V185 in photosystem II function in Synechocystis 6803 and Thermosynechococcus vestitus","authors":"Alain Boussac , Julien Sellés , Miwa Sugiura , Robert L. Burnap","doi":"10.1016/j.bbabio.2025.149550","DOIUrl":"10.1016/j.bbabio.2025.149550","url":null,"abstract":"<div><div>The effects of D1-V185T and D1-V185N mutations in Photosystem II (PSII) from <em>Thermosynechococcus vestitus</em> (formerly <em>T. elongatus</em>) and <em>Synechocystis</em> 6803, respectively, were studied using both EPR and optical kinetics. EPR spectroscopy reveals the presence of a mixture of a S<sub>2</sub> state in a high spin configuration (S<sub>2</sub><sup>HS</sup>) and in a low spin configuration (S<sub>2</sub><sup>LS</sup>) in both mutants. In contrast to the S<sub>2</sub><sup>HS</sup> in the wild type, the S<sub>2</sub><sup>HS</sup> state in the D1-V185T mutant does not progress to the S<sub>3</sub> state at 198 K. This inability is likely due to alterations in the protonation state and hydrogen-bonding network around the Mn<sub>4</sub>CaO<sub>5</sub> cluster. Optical studies show that these mutations significantly affect proton release during the S<sub>3</sub>-to-S<sub>0</sub> transition. While the initial fast proton release associated with Tyr<sub>Z</sub><sup>●</sup> formation remains unaffected within the resolution of our measurements, the second, and slower, proton release is delayed, suggesting that the mutations disrupt the hydrogen-bonding interactions necessary for efficient deprotonation of substrate water (O6). This disruption in proton transfer also correlates with slower water exchange in the S<sub>3</sub> state, likely due to non-native hydrogen bonds introduced by the threonine or asparagine side chains at position 185. These findings point to a critical role of D1-V185 in regulating both proton transfer dynamics and water binding, underscoring a complex interplay between structural and functional changes in PSII.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149550"},"PeriodicalIF":3.4,"publicationDate":"2025-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143517175","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Engineering of thermal stability in the recombinant xanthorhodopsin from Salinibacter ruber 重组橡胶盐碱菌黄杉质热稳定性的工程研究

IF 3.4 2区生物学

Biochimica et Biophysica Acta-Bioenergetics Pub Date : 2025-02-18 DOI: 10.1016/j.bbabio.2025.149547

Lada E. Petrovskaya , Vadim A. Bolshakov , Evgeniy P. Lukashev , Elena A. Kryukova , Eugene G. Maksimov , Andrei B. Rubin , Dmitriy A. Dolgikh , Sergei P. Balashov , Mikhail P. Kirpichnikov

{"title":"Engineering of thermal stability in the recombinant xanthorhodopsin from Salinibacter ruber","authors":"Lada E. Petrovskaya , Vadim A. Bolshakov , Evgeniy P. Lukashev , Elena A. Kryukova , Eugene G. Maksimov , Andrei B. Rubin , Dmitriy A. Dolgikh , Sergei P. Balashov , Mikhail P. Kirpichnikov","doi":"10.1016/j.bbabio.2025.149547","DOIUrl":"10.1016/j.bbabio.2025.149547","url":null,"abstract":"<div><div>Solubilization in detergents is a widely used technique for the isolation of membrane proteins and the study of their properties. Unfortunately, protein stability in detergent micelles can sometimes be compromised. We encountered this issue with xanthorhodopsin (XR) from <em>Salinibacter ruber</em>, which had been previously engineered for expression in <em>Escherichia coli</em> cells. To explore the factors affecting stability and to enhance thermal stability of recombinant XR preparations following solubilization of membranes using n-dodecyl-β-D-maltopyranoside and nickel-affinity chromatography, we developed a series of hybrid proteins based on the homology between XR and a stable rhodopsin from <em>Gloeobacter violaceus</em> (GR). Functional studies of these hybrids and measurements of their melting temperatures revealed the structural elements of XR that account for its notable difference in stability compared to GR, despite their high overall homology of approximately 50 % identical residues.</div><div>In particular, XR variants with an engineered loop between transmembrane helices D and E, similar to that in GR, demonstrated enhanced stability. However, we found that replacing the DE loop affects carotenoid binding. Additionally, two hybrid proteins containing the C and D helices from GR exhibited increased stability as well as improved photocycle and proton transport rates. In conclusion, we have demonstrated that optimizing the amino acid sequence of xanthorhodopsin from <em>S. ruber</em> based on its homology with <em>Gloeobacter</em> rhodopsin is an effective approach to enhance its thermal stability in vitro and improve its potential for optogenetic applications.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149547"},"PeriodicalIF":3.4,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143464421","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Defining the direct electron transfer connection between alternative complex III and cytochrome oxidase in Flavobacterium johnsoniae 确定琼氏黄杆菌中选择性络合物III与细胞色素氧化酶之间的直接电子转移联系。

IF 3.4 2区生物学

Biochimica et Biophysica Acta-Bioenergetics Pub Date : 2025-02-14 DOI: 10.1016/j.bbabio.2025.149548

Katarzyna Lorencik , Robert Ekiert , Rafał Pietras , Joanna Ner-Kluza , Małgorzata Hopciaś , Artur Osyczka

{"title":"Defining the direct electron transfer connection between alternative complex III and cytochrome oxidase in Flavobacterium johnsoniae","authors":"Katarzyna Lorencik , Robert Ekiert , Rafał Pietras , Joanna Ner-Kluza , Małgorzata Hopciaś , Artur Osyczka","doi":"10.1016/j.bbabio.2025.149548","DOIUrl":"10.1016/j.bbabio.2025.149548","url":null,"abstract":"<div><div>Alternative complex III (ACIII) is an enzyme of electron transport chains in some bacterial species. ACIII, like cytochrome <em>bc</em> enzymes, oxidizes quinol and transfers electrons from quinol to electron acceptors located outside the membrane. Various proteins can functionally link ACIII with other enzymes. The structure of ACIII from <em>Flavobacterium johnsoniae</em> suggests that in this bacterium the membrane-anchored mobile mono-heme cytochrome <em>c</em> domain (mdA) of the ActA subunit of ACIII provides means for its connection with cytochrome <em>aa</em><sub>3</sub> oxidase. Here, using a recently-developed genetic system for ACIII, we revealed that ACIII mutant deprived of mdA does not exhibit electron transfer activity towards cytochrome <em>aa</em><sub>3</sub> oxidase in the cells and in the isolated membranes. These results indicate that mdA is the only carrier of electrons between the pentaheme core of ActA and cytochrome <em>aa</em><sub>3</sub> oxidase. In addition, we heterologously expressed and purified mdA and ActE (another mono-heme subunit of ACIII) from <em>Escherichia coli</em> to identify the redox midpoint potentials of the hemes in these two domains. The obtained values analyzed in the context of the whole titration profiles of native ACIII and ACIII deprived of mdA provide first insights into the arrangement of heme redox potentials in the seven-heme chain formed by the ActA/ActE assembly.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149548"},"PeriodicalIF":3.4,"publicationDate":"2025-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143434190","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Corrigendum to “Structural robustness of the NADH binding site in NADH: Ubiquinone oxidoreductase (complex I)” [Biochim. Biophys. Acta (BBA) – Bioenerg. (2024)/149491] “NADH中NADH结合位点的结构稳健性：泛醌氧化还原酶（复合体I）”的更正[Biochim。Biophys。学报（工商管理学士）-生物能源。(2024) / 149491)。

IF 3.4 2区生物学

Biochimica et Biophysica Acta-Bioenergetics Pub Date : 2025-02-14 DOI: 10.1016/j.bbabio.2025.149549

Sanaz Göppert-Asadollahpour, Daniel Wohlwend, Thorsten Friedrich

引用次数: 0

Structural study of the chlorophyll between Lhca8 and PsaJ in an Antarctica green algal photosystem I-LHCI supercomplex revealed by its atomic structure 南极绿藻光系统I-LHCI超配合物中Lhca8和PsaJ之间叶绿素的结构研究

IF 3.4 2区生物学

Biochimica et Biophysica Acta-Bioenergetics Pub Date : 2025-02-11 DOI: 10.1016/j.bbabio.2025.149543

Pi-Cheng Tsai, Koji Kato, Jian-Ren Shen, Fusamichi Akita

{"title":"Structural study of the chlorophyll between Lhca8 and PsaJ in an Antarctica green algal photosystem I-LHCI supercomplex revealed by its atomic structure","authors":"Pi-Cheng Tsai, Koji Kato, Jian-Ren Shen, Fusamichi Akita","doi":"10.1016/j.bbabio.2025.149543","DOIUrl":"10.1016/j.bbabio.2025.149543","url":null,"abstract":"<div><div><em>Coccomyxa subellipsoidea</em> is an oleaginous, non-motile unicellular green microalga isolated from Antarctica, and is an attractive candidate for CO<sub>2</sub> fixation and biomass production. <em>C. subellipsoidea</em> is the first polar green alga whose genome has been sequenced. Understanding the structure of photosystems from <em>C. subellipsoidea</em> can provide more information about the conversion of light energy into chemical energy under extreme environments. Photosystems I (PSI) is one of the two photosystems highly conserved from cyanobacteria to vascular plants, and associates with a large amount of outer light-harvesting complex (LHC) which absorb light energy and transfer them to the core complex. Here, we determined the structure of the PSI-10 LHCIs and PSI-8 LHCIs supercomplexes from <em>C. subellipsoidea</em> at 1.92 Å and 2.06 Å resolutions by cryo-electron microscopy, respectively. The supercomplex is similar to PSI-LHCI from other green algae, whereas a large amount of water molecules is observed in our structure because of the high-resolution map. Two novel chlorophylls (Chls), Chl <em>a</em>321 in Lhca4 and Chl <em>a</em>314 in Lhca8, are observed at the lumenal side in our structure, in which Lhca8-Chl <em>a</em>314 provides a potential excitation energy transfer (EET) pathway between the inner-belt of LHCI and the core at the lumenal side. A total of three major EET pathways from LHCIs to PSI core are proposed, and <em>C. subellipsoidea</em> might adapt to the extreme environment by transferring energy in these three different EET pathways instead of by two major pathways proposed in other organisms.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149543"},"PeriodicalIF":3.4,"publicationDate":"2025-02-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143402854","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Mitochondrial potassium channels: New properties and functions 线粒体钾通道：新的性质和功能

IF 3.4 2区生物学

Biochimica et Biophysica Acta-Bioenergetics Pub Date : 2025-02-09 DOI: 10.1016/j.bbabio.2025.149546

Adam Szewczyk , Piotr Bednarczyk , Bogusz Kulawiak , Monika Żochowska , Barbara Kalenik , Joanna Lewandowska , Karolina Pytlak , Shur Gałecka , Antoni Wrzosek , Piotr Koprowski

{"title":"Mitochondrial potassium channels: New properties and functions","authors":"Adam Szewczyk , Piotr Bednarczyk , Bogusz Kulawiak , Monika Żochowska , Barbara Kalenik , Joanna Lewandowska , Karolina Pytlak , Shur Gałecka , Antoni Wrzosek , Piotr Koprowski","doi":"10.1016/j.bbabio.2025.149546","DOIUrl":"10.1016/j.bbabio.2025.149546","url":null,"abstract":"<div><div>Mitochondria are recently implicated in phenomena such as cytoprotection, cellular senescence, tumor metabolism, and inflammation. The basis of these processes relies on biochemical functions of mitochondria such as the synthesis of reactive oxygen species or biophysical properties such as the integrity of the inner mitochondrial membrane. The transport of potassium cations plays an important role in all these events. The K<sup>+</sup> influx is mediated by potassium channels present in the inner mitochondrial membrane. In this article, we present an overview of our new findings on the properties of mitochondrial large-conductance calcium-activated and mitochondrial ATP-regulated potassium channels. This concerns the role of mitochondrial potassium channels in cellular senescence, and interactions with other mitochondrial proteins or small molecules such as quercetin, hemin, and hydrogen sulfide. We also discuss the prospects of research on potassium channels present in mitochondria.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149546"},"PeriodicalIF":3.4,"publicationDate":"2025-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143376895","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural integrity and near-infrared absorption of the LH1 complex of Thermochromatium tepidum: Influence from the C-terminal lysine residues of LH1 α-polypeptide 温染菌LH1配合物的结构完整性和近红外吸收：LH1 α-多肽c端赖氨酸残基的影响

IF 3.4 2区生物学

Biochimica et Biophysica Acta-Bioenergetics Pub Date : 2025-02-09 DOI: 10.1016/j.bbabio.2025.149545

Yi-Hao Yan , Yu-Qian Li , Mei-Juan Zou , Long-Jiang Yu , Jian-Ping Zhang

{"title":"Structural integrity and near-infrared absorption of the LH1 complex of Thermochromatium tepidum: Influence from the C-terminal lysine residues of LH1 α-polypeptide","authors":"Yi-Hao Yan , Yu-Qian Li , Mei-Juan Zou , Long-Jiang Yu , Jian-Ping Zhang","doi":"10.1016/j.bbabio.2025.149545","DOIUrl":"10.1016/j.bbabio.2025.149545","url":null,"abstract":"<div><div>The light-harvesting complex 1-reaction center (LH1-RC) photosystem of the thermophilic purple sulfur bacterium <em>Thermochromatium</em> (<em>Tch</em>.) <em>tepidum</em> exhibits a near-infrared LH1-Q<sub>y</sub> absorption band at 915 nm as regulated by binding calcium ions (Ca<sup>2+</sup>). To further explore the possible involvement of the C-terminal lysine residues of the LH1 α-polypeptide, we have genetically engineered a <em>Rhodospirillum rubrum</em> mutant strain to yield the site-directed modifications of the terminal α-Lys60 and α-Lys61 residues of <em>Tch</em>. <em>tepidum</em> LH1 α-polypeptide. Four of the LH1 mutants exhibit a subtle blue shift of 3 nm upon deletion or substitution of the lysine residues, however, they display over 40 nm blue shifts upon Ca<sup>2+</sup> removal by ethylene diamine tetraacetic acid (EDTA) treatment. Spectral properties of native <em>Tch</em>. <em>tepidum</em> LH1-RC, the LH1-only, and the mutant LH1-only complexes are compared on a structural basis, which allows us to conclude that the C-terminal lysine residues and the Ca<sup>2+</sup> binding <em>synergistically</em> affect the structural integrity and the LH1-Q<sub>y</sub> spectral shift. This work demonstrates a methodology for the genetic manipulation of photosynthetic proteins lacking mutagenesis information, and may shed light on understanding the detailed structural factors involved in tuning the LH1-Q<sub>y</sub> absorption.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149545"},"PeriodicalIF":3.4,"publicationDate":"2025-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143378758","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Atypical absorption response to the trans-thylakoid electric field in the acidothermophilic red algae Cyanidioschyzon merolae and Galdieria partita 嗜酸嗜热红藻对类囊体反式电场的非典型吸收响应。

IF 3.4 2区生物学

Biochimica et Biophysica Acta-Bioenergetics Pub Date : 2025-02-07 DOI: 10.1016/j.bbabio.2025.149544

Guan-Lin Wu , Shin-Ying Tzeng , Benjamin Bailleul , Julien Sellés , You-Yuan Zhang , Han-Yi Fu

{"title":"Atypical absorption response to the trans-thylakoid electric field in the acidothermophilic red algae Cyanidioschyzon merolae and Galdieria partita","authors":"Guan-Lin Wu , Shin-Ying Tzeng , Benjamin Bailleul , Julien Sellés , You-Yuan Zhang , Han-Yi Fu","doi":"10.1016/j.bbabio.2025.149544","DOIUrl":"10.1016/j.bbabio.2025.149544","url":null,"abstract":"<div><div>An absorption change responding to the change in the trans-thylakoid electric field (Δψ), also known as the electrochromic shift (ECS) signal, is widely used to probe multiple photosynthetic processes. The ECS signals either display a linear response of absorption changes to Δψ, independent of the trans-thylakoid electric field preexisting before actinic light (ψ<sub>O</sub>), or a quadratic response, dependent on ψ<sub>O</sub>. In the acidothermophilic red algae <em>Cyanidioschyzon merolae</em> and <em>Galdieria partita</em>, the absorption changes induced by single turnover saturating light flashes were affected by external pH. The effects of elevated external pH on the flash-induced absorption changes were explained by diminished ψ<sub>O</sub>, as shown with the treatment of ionophores. We identified three contributions to the absorption changes: c-type cytochrome oxidized-minus-reduced signal and ECS signals showing both ψ<sub>O</sub>-dependent and ψ<sub>O</sub>-independent responses. Based on this, we could reveal that the effects of elevated external pH on the flash-induced absorption changes were due to variations of ψ<sub>O</sub>, which in turn changed the contribution of the ψ<sub>O</sub>-dependent ECS, as shown with the treatment of ionophores. Further analysis revealed that the ψ<sub>O</sub>-dependent ECS signal exhibited a quadratic response to Δψ at low ψ<sub>O</sub>, but the quadraticity was lost at higher ψ<sub>O</sub>, providing insights for comprehending the atypical nature of the ECS signal. Our approach to identifying the ψ<sub>O</sub>-dependent and ψ<sub>O</sub>-independent ECS signals enables the ECS-based measurements for further investigation of the bioenergetics of electron and proton transport in red algae.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149544"},"PeriodicalIF":3.4,"publicationDate":"2025-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143383713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Circadian clockwork controls the balance between mitochondrial turnover and dynamics: What is life … without time marking? 生物钟控制着线粒体更新和动态之间的平衡：没有时间标记的生命是什么？

IF 3.4 2区生物学

Biochimica et Biophysica Acta-Bioenergetics Pub Date : 2025-01-27 DOI: 10.1016/j.bbabio.2025.149542

Olga Cela , Rosella Scrima , Michela Rosiello , Consiglia Pacelli , Claudia Piccoli , Mirko Tamma , Francesca Agriesti , Gianluigi Mazzoccoli , Nazzareno Capitanio

{"title":"Circadian clockwork controls the balance between mitochondrial turnover and dynamics: What is life … without time marking?","authors":"Olga Cela , Rosella Scrima , Michela Rosiello , Consiglia Pacelli , Claudia Piccoli , Mirko Tamma , Francesca Agriesti , Gianluigi Mazzoccoli , Nazzareno Capitanio","doi":"10.1016/j.bbabio.2025.149542","DOIUrl":"10.1016/j.bbabio.2025.149542","url":null,"abstract":"<div><div>Circadian rhythms driven by biological clocks regulate physiological processes in all living organisms by anticipating daily geophysical changes, thus enhancing environmental adaptation. Time-resolved serial multi-omic analyses in vivo, ex vivo, and in synchronized cell cultures have revealed rhythmic changes in the transcriptome, proteome, and metabolome, involving up to 50 % of the mammalian genome. Mitochondrial oxidative metabolism is central to cellular bioenergetics, and many nuclear genes encoding mitochondrial proteins exhibit both circadian and ultradian oscillatory expression. However, studies on mitochondrial DNA (mtDNA) gene expression remain incomplete. Using a well-established in vitro synchronization protocol, we investigated the time-resolved expression of mtDNA genes coding for respiratory chain complex subunits, revealing a rhythmic profile dependent on BMAL1, the master circadian clock transcription factor. Additionally, the expression of genes coding for key mitochondrial biogenesis transcription factors, PGC1a, NRF1, and TFAM, showed BMAL1-dependent circadian oscillations. Notably, LC3-II, involved in mitophagy, displayed a similar in-phase circadian expression, thereby maintaining stable respiratory chain complex levels. Moreover, we found that simultaneous mitochondrial biogenesis and degradation occur in a coordinated manner with cycles in organelle dynamics, leading to rhythmic changes in mitochondrial fission and fusion. This study provides new insights into circadian clock regulation of mitochondrial turnover, emphasizing the importance of temporal regulation in cellular metabolism. Understanding these mechanisms opens potential therapeutic avenues for targeting mitochondrial dysfunctions and related metabolic disorders.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149542"},"PeriodicalIF":3.4,"publicationDate":"2025-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143069253","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Commentary: Why do many cell biology papers contain fundamental bioenergetic errors? 评论：为什么许多细胞生物学论文包含基本的生物能错误？

IF 3.4 2区生物学

Biochimica et Biophysica Acta-Bioenergetics Pub Date : 2025-01-17 DOI: 10.1016/j.bbabio.2025.149541

David G. Nicholls

引用次数: 0