Biochemical Society transactions最新文献

Mechanisms of heme transport in the mitochondria. 线粒体中血红素运输的机制。

IF 3.8 3区生物学

Biochemical Society transactions Pub Date : 2025-05-29 DOI: 10.1042/BST20253013

Saieeda Fabia Ali, Adrianna E White, Amy Medlock, Oleh Khalimonchuk

引用次数: 0

Insights into the role of collided ribosomes during the activation of the integrated stress response. 在综合应激反应的激活过程中碰撞核糖体的作用。

IF 3.8 3区生物学

Biochemical Society transactions Pub Date : 2025-05-28 DOI: 10.1042/BST20253034

Ankanahalli N Nanjaraj Urs, Lucas Kim, Hani S Zaher

{"title":"Insights into the role of collided ribosomes during the activation of the integrated stress response.","authors":"Ankanahalli N Nanjaraj Urs, Lucas Kim, Hani S Zaher","doi":"10.1042/BST20253034","DOIUrl":"https://doi.org/10.1042/BST20253034","url":null,"abstract":"Mechanisms that regulate and reprogram gene expression are particularly important under stress conditions. The integrated stress response (ISR) signaling pathway is one such pro-survival and adaptive mechanism conserved in eukaryotes. The ISR is characterized by the activation of protein kinases that phosphorylate the eukaryotic initiation factor 2α (eIF2α) in response to several stress conditions, including nutrient deprivation, viral infection, and protein misfolding. Phosphorylation of eIF2α results in global inhibition of translation, while promoting the translation of a few pro-survival genes. Here, we focus on the mechanism of activation of the eIF2α kinase general control nonderepressible 2 (Gcn2). The protein was initially discovered in yeast more than four decades ago, and it was proposed to respond to amino acid starvation through the accumulation of deacylated tRNAs. However, more recent studies have changed our understanding of its activation and suggest a direct role for ribosome stalling and collisions in the process. In this review, we discuss the classical model for the tRNA-mediated activation of GCN2 and the recent shift in this model to accommodate the observations that wide-ranging translational stresses trigger its activation.","PeriodicalId":8841,"journal":{"name":"Biochemical Society transactions","volume":" ","pages":""},"PeriodicalIF":3.8,"publicationDate":"2025-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144172493","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Exploring the interaction dynamics of eukaryotic translation initiation factor 2. 真核生物翻译起始因子2相互作用动力学研究。

IF 3.8 3区生物学

Biochemical Society transactions Pub Date : 2025-05-23 DOI: 10.1042/BST20253022

Assen Marintchev

{"title":"Exploring the interaction dynamics of eukaryotic translation initiation factor 2.","authors":"Assen Marintchev","doi":"10.1042/BST20253022","DOIUrl":"https://doi.org/10.1042/BST20253022","url":null,"abstract":"Eukaryotic translation initiation typically involves recruitment of the 43S ribosomal pre-initiation complex (PIC) to the 5'-end of the mRNA to form the 48S PIC, followed by scanning in search of a start codon in a favorable nucleotide complex. The start codon is recognized through base-pairing with the anticodon of the initiator Met-tRNAi. The stringency of start codon selection controls the probability of initiation from a start codon in a suboptimal nucleotide context. Met-tRNAi itself is recruited to the 43S PIC by the eukaryotic translation initiation factor 2 (eIF2), in the form of the eIF2-GTP•Met-tRNAi ternary complex (TC). GTP hydrolysis by eIF2, promoted by its GTPase-activating protein eIF5, leads to the release of eIF2-GDP from the PIC. Recycling of eIF2-GDP to TC is promoted by the guanine nucleotide exchange factor eIF2B. Its inhibition by a number of stress factors triggers the integrated stress response (ISR). This review describes the recent advances in elucidating the interactions of eIF2 and its partners, with an emphasis on the timing and dynamics of their binding to, and release from the PIC. Special attention is given to the regulation of the stringency of start codon selection and the ISR. The discussion is mostly limited to translation initiation in mammals and budding yeast.","PeriodicalId":8841,"journal":{"name":"Biochemical Society transactions","volume":" ","pages":""},"PeriodicalIF":3.8,"publicationDate":"2025-05-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144135997","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Emerging tools and methods to study cell signalling mediated by branched ubiquitin chains. 研究分支泛素链介导的细胞信号传导的新兴工具和方法。

IF 3.8 3区生物学

Biochemical Society transactions Pub Date : 2025-05-16 DOI: 10.1042/BST20253015

Matthew R McFarland, Yogesh Kulathu

引用次数: 0

Advances in ribosome profiling technologies. 核糖体分析技术进展。

IF 3.8 3区生物学

Biochemical Society transactions Pub Date : 2025-05-16 DOI: 10.1042/BST20253061

Kotaro Tomuro, Shintaro Iwasaki

引用次数: 0

Advances in understanding the mechanisms of the human papillomavirus oncoproteins. 人乳头瘤病毒癌蛋白机制的研究进展。

IF 3.8 3区生物学

Biochemical Society transactions Pub Date : 2025-05-16 DOI: 10.1042/BST20253041

Denise Ijeoma Obanya, Louisa M Wootton, Ethan L Morgan

引用次数: 0

Insights into the synchronization between DNA replication and parental histone recycling. DNA复制和亲本组蛋白循环同步的见解。

IF 3.8 3区生物学

Biochemical Society transactions Pub Date : 2025-05-14 DOI: 10.1042/BST20253014

Xiaorong Tang, Yuan Yao, Gang Li, Haiyun Gan

引用次数: 0

Cdk activation by phosphorylation: linking growth signals to cell cycle control. 磷酸化激活Cdk：将生长信号与细胞周期控制联系起来。

IF 3.8 3区生物学

Biochemical Society transactions Pub Date : 2025-05-09 DOI: 10.1042/BST20253004

Heidi M Blank, Eun-Gyu No, Michael Polymenis

引用次数: 0

S-acylation in apoptotic and non-apoptotic cell death: a central regulator of membrane dynamics and protein function. 凋亡和非凋亡细胞死亡中的s -酰化：膜动力学和蛋白质功能的中心调节因子。

IF 3.8 3区生物学

Biochemical Society transactions Pub Date : 2025-04-29 DOI: 10.1042/BST20253012

Rojae Manhertz-Patterson, G Ekin Atilla-Gokcumen

{"title":"S-acylation in apoptotic and non-apoptotic cell death: a central regulator of membrane dynamics and protein function.","authors":"Rojae Manhertz-Patterson, G Ekin Atilla-Gokcumen","doi":"10.1042/BST20253012","DOIUrl":"10.1042/BST20253012","url":null,"abstract":"Protein lipidation is a collection of important post-translational modifications that modulate protein localization and stability. Protein lipidation affects protein function by facilitating interactions with cellular membranes, changing the local environment of protein interactions. Among these modifications, S-acylation has emerged as a key regulator of various cellular processes, including different forms of cell death. In this mini-review, we highlight the role of S-acylation in apoptosis and its emerging contributions to necroptosis and pyroptosis. While traditionally associated with the incorporation of palmitic acid (palmitoylation), recent findings indicate that other fatty acids can also participate in S-acylation, expanding its functional repertoire. In apoptosis, S-acylation influences the localization and function of key regulators such as Bcl-2-associated X protein and other proteins modulating their role in mitochondrial permeabilization and death receptor signaling. Similarly, in necroptosis, S-acylation of mixed lineage kinase domain-like protein (MLKL) with palmitic acid and very long-chain fatty acids enhances membrane binding and membrane permeabilization, contributing to cell death and inflammatory responses. Recent studies also highlight the role of S-acylation in pyroptosis, where S-acylated gasdermin D facilitates membrane localization and pore assembly upon inflammasome activation. Blocking palmitoylation has shown to suppress pyroptosis and cytokine release, reducing inflammatory activity and tissue damage in septic models. Collectively, these findings underscore S-acylation as a shared and important regulatory mechanism across cell death pathways affecting membrane association of key signaling proteins and membrane dynamics, and offer insights into the spatial and temporal control of protein function.","PeriodicalId":8841,"journal":{"name":"Biochemical Society transactions","volume":"53 2","pages":""},"PeriodicalIF":3.8,"publicationDate":"2025-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143970451","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Functions and mechanisms of eukaryotic RNA-guided programmed DNA elimination. 真核生物rna引导的程序化DNA消除的功能和机制。

IF 3.8 3区生物学

Biochemical Society transactions Pub Date : 2025-04-29 DOI: 10.1042/BST20253006

Bozhidar-Adrian Stefanov, Mariusz Nowacki

{"title":"Functions and mechanisms of eukaryotic RNA-guided programmed DNA elimination.","authors":"Bozhidar-Adrian Stefanov, Mariusz Nowacki","doi":"10.1042/BST20253006","DOIUrl":"10.1042/BST20253006","url":null,"abstract":"Many eukaryotic organisms, from ciliates to mammals, employ programmed DNA elimination during their postmeiotic reproduction. The process removes specific regions from the somatic DNA and has broad functions, including the irreversible silencing of genes, sex determination, and genome protection from transposable elements or integrating viruses. Multiple mechanisms have evolved that explain the sequence selectivity of the process. In some cases, the eliminated sequences lack centromeres and are flanked by conserved sequence motifs that are specifically recognized and cleaved by designated nucleases. Upon cleavage, all DNA fragments that lack centromeres are lost during the following mitosis. Alternatively, specific sequences can be destined for elimination by complementary small RNAs (sRNAs) as in some ciliates. These sRNAs enable a PIWI-mediated recruitment of chromatin remodelers, followed up by the precise positioning of a cleavage complex formed from a transposase like PiggyBac or Tc1. Here, we review the known molecular interplay of the cellular machinery that is involved in precise sRNA-guided DNA excision, and additionally, we highlight prominent knowledge gaps. We focus on the modes through which sRNAs enable the precise localization of the cleavage complex, and how the nuclease activity is controlled to prevent off-target cleavage. A mechanistic understanding of this process could enable the development of novel eukaryotic genome editing tools.","PeriodicalId":8841,"journal":{"name":"Biochemical Society transactions","volume":"53 2","pages":""},"PeriodicalIF":3.8,"publicationDate":"2025-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143963913","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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