Pub Date : 2026-02-01DOI: 10.1016/j.tibs.2025.12.010
Alice Chanteau , Fabien Nogué , Rajeev Kumar
BReast CAncer 2 (BRCA2) safeguards genome integrity across eukaryotes by facilitating DNA repair. A defining feature of BRCA2 orthologs is their ability to bind to DNA. Here, we highlight emerging roles of multiple DNA-binding modules that act in a complementary manner and contribute uniquely to BRCA2 functions.
{"title":"DNA binding is a defining feature of BRCA2 orthologs","authors":"Alice Chanteau , Fabien Nogué , Rajeev Kumar","doi":"10.1016/j.tibs.2025.12.010","DOIUrl":"10.1016/j.tibs.2025.12.010","url":null,"abstract":"<div><div>BReast CAncer 2 (BRCA2) safeguards genome integrity across eukaryotes by facilitating DNA repair. A defining feature of BRCA2 orthologs is their ability to bind to DNA. Here, we highlight emerging roles of multiple DNA-binding modules that act in a complementary manner and contribute uniquely to BRCA2 functions.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 2","pages":"Pages 103-106"},"PeriodicalIF":11.0,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146016810","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/S0968-0004(26)00014-9
{"title":"Subscription and Copyright Information","authors":"","doi":"10.1016/S0968-0004(26)00014-9","DOIUrl":"10.1016/S0968-0004(26)00014-9","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 2","pages":"Page e1"},"PeriodicalIF":11.0,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146116274","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.tibs.2025.11.009
Ana Lago-Maciel , Marcello Herzog , Johannes G. Rebelein
Nitrogenases are the only enzymes capable of converting atmospheric nitrogen into bioavailable ammonia, an essential process for all life on Earth. Early ancestors of bona fide nitrogenases and their maturases gave rise to several structural homologues with diverse functions. The nitrogen fixation-like enzyme superfamily comprises ancient metalloproteins involved in elemental processes that range from the biosynthesis of bacteriochlorophyll in bacterial photosynthesis to the biosynthesis of cofactor F430 in archaeal methanogenesis. Recently, new functions of nitrogenase-like enzymes in sulfur scavenging were discovered and have spurred interest due to the simultaneous production of small hydrocarbons. Here we explore the structural and functional diversity of the nitrogen fixation-like enzyme superfamily and its potential for the production of chemical building blocks beyond ammonia formation.
{"title":"Functional insights into the nitrogenase-like enzyme superfamily","authors":"Ana Lago-Maciel , Marcello Herzog , Johannes G. Rebelein","doi":"10.1016/j.tibs.2025.11.009","DOIUrl":"10.1016/j.tibs.2025.11.009","url":null,"abstract":"<div><div>Nitrogenases are the only enzymes capable of converting atmospheric nitrogen into bioavailable ammonia, an essential process for all life on Earth. Early ancestors of <em>bona fide</em> nitrogenases and their maturases gave rise to several structural homologues with diverse functions. The nitrogen fixation-like enzyme superfamily comprises ancient metalloproteins involved in elemental processes that range from the biosynthesis of bacteriochlorophyll in bacterial photosynthesis to the biosynthesis of cofactor F<sub>430</sub> in archaeal methanogenesis. Recently, new functions of nitrogenase-like enzymes in sulfur scavenging were discovered and have spurred interest due to the simultaneous production of small hydrocarbons. Here we explore the structural and functional diversity of the nitrogen fixation-like enzyme superfamily and its potential for the production of chemical building blocks beyond ammonia formation.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 2","pages":"Pages 187-202"},"PeriodicalIF":11.0,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145896040","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.tibs.2025.12.003
Tamor Khan
{"title":"Musings of a lab janitor: AI shenanigans","authors":"Tamor Khan","doi":"10.1016/j.tibs.2025.12.003","DOIUrl":"10.1016/j.tibs.2025.12.003","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 2","pages":"Page 203"},"PeriodicalIF":11.0,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146116275","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.tibs.2025.10.005
Cameron Gibson , Idin Lantz , Michael Downey
Lysine acetylation is a post-translational modification (PTM) that is traditionally studied as a modifier of histones. In recent years, nonhistone protein acetylation has also emerged as a ubiquitous modification in eukaryotes. Recent advances in mass spectrometry (MS) workflows suggest that a majority of proteins are acetylated at some point during their life cycle. However, only a few of these acetylations have been studied for their functional significance. Here, we review the function of acetylations on key nonhistone proteins involved in chromatin remodeling and DNA damage repair, protein homeostasis, and metabolic coordination of the cell cycle in Saccharomyces cerevisiae. We discuss the diverse roles of acetylation in regulating these pathways, while highlighting emerging themes and open questions in the field.
{"title":"Emerging functions for nonhistone protein acetylation in budding yeast","authors":"Cameron Gibson , Idin Lantz , Michael Downey","doi":"10.1016/j.tibs.2025.10.005","DOIUrl":"10.1016/j.tibs.2025.10.005","url":null,"abstract":"<div><div>Lysine acetylation is a post-translational modification (PTM) that is traditionally studied as a modifier of histones. In recent years, nonhistone protein acetylation has also emerged as a ubiquitous modification in eukaryotes. Recent advances in mass spectrometry (MS) workflows suggest that a majority of proteins are acetylated at some point during their life cycle. However, only a few of these acetylations have been studied for their functional significance. Here, we review the function of acetylations on key nonhistone proteins involved in chromatin remodeling and DNA damage repair, protein homeostasis, and metabolic coordination of the cell cycle in <em>Saccharomyces cerevisiae</em>. We discuss the diverse roles of acetylation in regulating these pathways, while highlighting emerging themes and open questions in the field.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 2","pages":"Pages 158-171"},"PeriodicalIF":11.0,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145494248","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.tibs.2025.11.010
Gaëlle Lescalet , Alberto David Delgado Monterroso , Rima Kochman , Stéphane Coulon , Alexandre Maréchal
The repetitive G-/C-rich nature of telomeres makes them potent obstacles to replicative DNA polymerases, eliciting a state of replication stress during genome duplication. Within replisomes and as part of the shelterin complex, numerous single-stranded DNA (ssDNA)–binding proteins (SSBPs) help maintain telomere homeostasis by protecting specific telomeric structures and managing replication stress. Underlining their critical roles, mutations in key ssDNA binders influence telomere length, cause telomeropathies, and/or act as drivers of cancer development. Here, we review recent findings on the roles of SSBPs and their coordination during telomere replication and elongation. We also present recent advances on ssDNA-binding factors and their regulators in alternative lengthening of telomeres (ALTs), highlighting how these findings may provide viable therapeutic targets in ALT cancers.
{"title":"Single-stranded DNA-binding proteins at healthy and diseased telomeres","authors":"Gaëlle Lescalet , Alberto David Delgado Monterroso , Rima Kochman , Stéphane Coulon , Alexandre Maréchal","doi":"10.1016/j.tibs.2025.11.010","DOIUrl":"10.1016/j.tibs.2025.11.010","url":null,"abstract":"<div><div>The repetitive G-/C-rich nature of telomeres makes them potent obstacles to replicative DNA polymerases, eliciting a state of replication stress during genome duplication. Within replisomes and as part of the shelterin complex, numerous single-stranded DNA (ssDNA)–binding proteins (SSBPs) help maintain telomere homeostasis by protecting specific telomeric structures and managing replication stress. Underlining their critical roles, mutations in key ssDNA binders influence telomere length, cause telomeropathies, and/or act as drivers of cancer development. Here, we review recent findings on the roles of SSBPs and their coordination during telomere replication and elongation. We also present recent advances on ssDNA-binding factors and their regulators in alternative lengthening of telomeres (ALTs), highlighting how these findings may provide viable therapeutic targets in ALT cancers.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 2","pages":"Pages 125-141"},"PeriodicalIF":11.0,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145931713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.tibs.2025.11.002
Denis Lacabanne , Jonathan J. Ruprecht , Maximilian Sichrovsky , Lucy R. Forrest , Vanessa Leone , Sotiria Tavoulari , Edmund R.S. Kunji
The mitochondrial pyruvate carrier (MPC), of the SLC54 family of solute carriers, has a critical role in eukaryotic energy metabolism by transporting pyruvate, the end-product of glycolysis, into the mitochondrial matrix. Recently, structures of the human MPC1/MPC2 and MPC1L/MPC2 heterodimers in the outward-open, occluded, and inward-open states have been determined by cryo-electron microscopy (cryo-EM) and by AlphaFold modeling. In this review we discuss the membrane orientation, substrate binding site properties, and structural features of the alternating access mechanism of the carrier, as well as the binding poses of three chemically distinct inhibitor classes, which exploit the same binding site in the outward-open state. These structural studies will support drug development efforts for the treatment of diabetes mellitus, neurodegeneration, metabolic dysfunction-associated steatotic liver disease (MASLD), and some types of cancers.
{"title":"Structural transport and inhibition mechanism of the mitochondrial pyruvate carrier","authors":"Denis Lacabanne , Jonathan J. Ruprecht , Maximilian Sichrovsky , Lucy R. Forrest , Vanessa Leone , Sotiria Tavoulari , Edmund R.S. Kunji","doi":"10.1016/j.tibs.2025.11.002","DOIUrl":"10.1016/j.tibs.2025.11.002","url":null,"abstract":"<div><div>The mitochondrial pyruvate carrier (MPC), of the SLC54 family of solute carriers, has a critical role in eukaryotic energy metabolism by transporting pyruvate, the end-product of glycolysis, into the mitochondrial matrix. Recently, structures of the human MPC1/MPC2 and MPC1L/MPC2 heterodimers in the outward-open, occluded, and inward-open states have been determined by cryo-electron microscopy (cryo-EM) and by AlphaFold modeling. In this review we discuss the membrane orientation, substrate binding site properties, and structural features of the alternating access mechanism of the carrier, as well as the binding poses of three chemically distinct inhibitor classes, which exploit the same binding site in the outward-open state. These structural studies will support drug development efforts for the treatment of diabetes mellitus, neurodegeneration, metabolic dysfunction-associated steatotic liver disease (MASLD), and some types of cancers.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 2","pages":"Pages 142-157"},"PeriodicalIF":11.0,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145695679","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.tibs.2025.12.005
Welder Alves da Silva , Auxiliadora Oliveira Martins , Moab Torres de Andrade , Wagner Luiz Araújo
Recent advances have highlighted the flexibility of the plant metabolic network to meet its requirements under specific environmental and physiological conditions. In their publication, Gashu et al. provided a more complete picture of how much photosynthetically assimilated carbon is channeled from photorespiration to one-carbon metabolism under different photorespiratory conditions.
{"title":"Fine-tuning the connection between photorespiration and one-carbon metabolism","authors":"Welder Alves da Silva , Auxiliadora Oliveira Martins , Moab Torres de Andrade , Wagner Luiz Araújo","doi":"10.1016/j.tibs.2025.12.005","DOIUrl":"10.1016/j.tibs.2025.12.005","url":null,"abstract":"<div><div>Recent advances have highlighted the flexibility of the plant metabolic network to meet its requirements under specific environmental and physiological conditions. In their publication, <span><span>Gashu <em>et al</em>.</span><svg><path></path></svg></span> provided a more complete picture of how much photosynthetically assimilated carbon is channeled from photorespiration to one-carbon metabolism under different photorespiratory conditions.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 2","pages":"Pages 100-102"},"PeriodicalIF":11.0,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146008327","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.tibs.2025.12.002
Ling-Ling Chen (陈玲玲) , Alicia J. Kowaltowski
{"title":"The past, present, and future of RNA biochemistry and mitochondrial research","authors":"Ling-Ling Chen (陈玲玲) , Alicia J. Kowaltowski","doi":"10.1016/j.tibs.2025.12.002","DOIUrl":"10.1016/j.tibs.2025.12.002","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 2","pages":"Pages 95-97"},"PeriodicalIF":11.0,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146116567","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/S0968-0004(26)00011-3
{"title":"Advisory Board and Contents","authors":"","doi":"10.1016/S0968-0004(26)00011-3","DOIUrl":"10.1016/S0968-0004(26)00011-3","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 2","pages":"Pages i-ii"},"PeriodicalIF":11.0,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146116713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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