bioRxiv - Molecular Biology最新文献_第4页

A nanobody-based approach to capture and visualize interactions of binary protein complexes in living cells 基于纳米抗体的捕捉和可视化活细胞中二元蛋白质复合物相互作用的方法

bioRxiv - Molecular Biology Pub Date : 2024-09-13 DOI: 10.1101/2024.09.12.612471

Nawal Hajj Sleiman, Julie Carnesecchi, Yunlong Jia, Frederic Delolme, Laurent Gilquin, Patrice Gouet, Samir Merabet

{"title":"A nanobody-based approach to capture and visualize interactions of binary protein complexes in living cells","authors":"Nawal Hajj Sleiman, Julie Carnesecchi, Yunlong Jia, Frederic Delolme, Laurent Gilquin, Patrice Gouet, Samir Merabet","doi":"10.1101/2024.09.12.612471","DOIUrl":"https://doi.org/10.1101/2024.09.12.612471","url":null,"abstract":"Protein function depends on interactions with other protein partners, ultimately leading to the formation of intricate protein-protein interaction (PPI) networks. These molecular networks (or interactomes) are formed progressively, each interaction influencing the next one. Accordingly, a same protein can lead to the formation of different interactomes depending on its first associated cofactor. Therefore, capturing PPIs of specific dimeric protein complexes is key for understanding the molecular rules underlying the diverse cell- and/or subcellular- functions of a bait protein of interest. Here, we introduce an innovative method called Bi-nano-ID that is based on bicolor bimolecular fluorescence complementation and the specific binding of a nanobody fused to a proximity-dependent biotinylating enzyme to tackle this issue. Bi-nano-ID was used to capture endogenous interactomes of the cytoplasmic TAZ/14-3-3e and nuclear TAZ/TEAD2 complexes, which are major downstream effectors of the Hippo signaling pathway. Among the different specific interactions, we revealed the role of a particular family of protease inhibitors for stabilizing and promoting the proliferative activity of TAZ/14-3-3e complexes in mesenchymal stem cells. Overall, our work establishes a novel sensitive method for capturing and visualizing specific interactions of binary bait protein complexes in human living cells.","PeriodicalId":501108,"journal":{"name":"bioRxiv - Molecular Biology","volume":"187 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142253416","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Cleavage site heterogeneity at the pre-mRNA 3'-untranslated region regulates gene expression 前 mRNA 3'- 非翻译区的裂解位点异质性调控基因表达

bioRxiv - Molecular Biology Pub Date : 2024-09-13 DOI: 10.1101/2024.09.11.612397

Feba Shaji, Jamshaid Ali, Rakesh S. Laishram

{"title":"Cleavage site heterogeneity at the pre-mRNA 3'-untranslated region regulates gene expression","authors":"Feba Shaji, Jamshaid Ali, Rakesh S. Laishram","doi":"10.1101/2024.09.11.612397","DOIUrl":"https://doi.org/10.1101/2024.09.11.612397","url":null,"abstract":"Endonucleolytic cleavage step of the pre-mRNA 3'-end processing is imprecise and results in heterogeneity of cleavage site (CS). On the contrary, we show that cleavage imprecision is tightly regulated leading to CS heterogeneity (CSH) and controls antioxidant response gene expression. CSH centres at a primary CS followed by subsidiary cleavages determined by the position of the CS. Globally and using targeted antioxidant mRNAs, we discovered an inverse relationship between the number of CS and the gene expression with highest cleavage efficiency from the primary CS. Strikingly, reducing CSH and increasing primary CS usage induces gene expression. Under oxidative stress (tBHQ, H2O2 or NaAsO2), CSH is decreased and the primary CS usage is stimulated that induces antioxidant response gene expression. Concomitantly, ectopic anti-oxidant protein expression from the primary CS or reduction in CSH imparts cellular oxidative stress tolerance. Genome-wide CS analysis of stress response genes also shows a concomitant result. We show that oxidative stress induces affinity/strength of cleavage complex assembly increasing the fidelity of cleavage at the primary CS thereby reducing CSH inducing antioxidant response.","PeriodicalId":501108,"journal":{"name":"bioRxiv - Molecular Biology","volume":"21 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142212724","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Development of a DNA-encoded library screening method DEL Zipper to empower the study of RNA-targeted chemical matter 开发 DNA 编码文库筛选方法 DEL Zipper，增强 RNA 靶向化学物质的研究能力

bioRxiv - Molecular Biology Pub Date : 2024-09-13 DOI: 10.1101/2024.09.13.612806

Zhongyao Ma, Bin Zou, Jiannan Zhao, Rui Zhang, Qiaoqiao Zhu, Xiaofeng Wang, Linan Xu, Xiang Gao, Xinyue Hu, Wei Feng, Wen Luo, Min Wang, Yunyun He, Zhifeng Yu, Weiren Cui, Qi Zhang, Letian Kuai, Wenji Su

引用次数: 0

Decoding Transcriptional Memory in Yeast Heat Shock and the Functional Implication of the RNA Binding Protein Mip6 解码酵母热休克中的转录记忆和 RNA 结合蛋白 Mip6 的功能含义

bioRxiv - Molecular Biology Pub Date : 2024-09-13 DOI: 10.1101/2024.09.12.612644

Susana Rodriguez-Navarro, Ana Tejada-Colon, Joan Serrano-Quilez, Carme Nuno-Cabanes

{"title":"Decoding Transcriptional Memory in Yeast Heat Shock and the Functional Implication of the RNA Binding Protein Mip6","authors":"Susana Rodriguez-Navarro, Ana Tejada-Colon, Joan Serrano-Quilez, Carme Nuno-Cabanes","doi":"10.1101/2024.09.12.612644","DOIUrl":"https://doi.org/10.1101/2024.09.12.612644","url":null,"abstract":"Cells not only adapt to environmental changes, but they also \"remember\" specific signals, allowing them to respond more rapidly to future stressors. This phenomenon, known as transcriptional memory, is orchestrated by a complex interplay of epigenetics, transcription regulators and RNA metabolism factors. Although transcriptional memory has been well-studied in various contexts, its role in the heat shock (HS) response of yeast remains largely unexplored. In our study, we delve into the dynamics of HS memory in wild-type yeast and a mip6Δ mutant, which lacks the RNA-binding protein Mip6. Notably, Mip6 has been shown to influence the expression of key stress-related genes and maintain low Msn2/4-dependent transcript levels under standard conditions. Our transcriptomic analysis offers novel insights into how yeast cells remember HS exposure. We uncover striking differences in gene expression patterns depending on whether genes are induced or repressed during HS memory. Furthermore, we find that an initial 15-minute heat shock triggers a response that becomes attenuated with just 5 additional minutes of stress. While the response kinetics between memory and non-memory conditions are similar, we report a subtle but important role for Mip6 in fine-tuning transcriptional memory and adaptation to heat stress. Biochemical and genetic evidence also suggests that Mip6 cooperates with alternative survival pathways independent of MSN2/4, and functionally interacts with the Rpd3 histone deacetylase complex, a key player in transcriptional memory and the HS response. These findings open up new avenues for understanding the molecular mechanisms behind heat stress adaptation in eukaryotes.","PeriodicalId":501108,"journal":{"name":"bioRxiv - Molecular Biology","volume":"24 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142253419","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Introduction of cytosine-5 DNA methylation sensitizes cells to oxidative damage 引入胞嘧啶-5 DNA甲基化可使细胞对氧化损伤敏感

bioRxiv - Molecular Biology Pub Date : 2024-09-13 DOI: 10.1101/2024.09.13.612259

Joanna Krwawicz, Caroline J Sheeba, Katie Hains, Thomas McMahon, Yimo Zhang, Skirmantas Kriaucionis, Peter Sarkies

{"title":"Introduction of cytosine-5 DNA methylation sensitizes cells to oxidative damage","authors":"Joanna Krwawicz, Caroline J Sheeba, Katie Hains, Thomas McMahon, Yimo Zhang, Skirmantas Kriaucionis, Peter Sarkies","doi":"10.1101/2024.09.13.612259","DOIUrl":"https://doi.org/10.1101/2024.09.13.612259","url":null,"abstract":"DNA methylation at the 5 position of cytosine (5mC) is an ancient epigenetic mark in eukaryotes. The levels of total 5mC vary enormously between different species, and the DNA methyltransferases that introduce 5mC have been repeatedly lost in several independent lineages. DNA methyltransferases are a threat to genomic stability due to the increased mutagenicity of 5mC bases and the propensity of DNA methyltransferases themselves to introduce DNA alkylation damage as an off-target effect. However, whether alkylation damage explains why 5mC is frequently lost in evolution is unclear. Here we tested the fitness consequences of DNA methyltransferase-induced alkylation damage by introducing a eukaryotic-like 5mC system into E. coli. We showed that introducing 5mC genome-wide leads to increased sensitivity to alkylating agents, which is strongly enhanced by removal of the 3mC repair enzyme AlkB. Unexpectedly, we discovered that 5mC introduction led to increased sensitivity to oxidative stress. We showed that this is due to increased formation of reactive oxygen in the presence of 5mC. We determined that reactive oxygen species led to non-enzymatic oxidation of 5mC, producing modified cytosines such as 5fC that are recognised as DNA base damage in E. coli. Overall, our work identifies increased sensitivity to oxidative stress, as well as alkylating agents, as a negative consequence of genome-wide 5mC. Oxidative stress is frequently encountered by organisms in their environment, thus offering a plausible reason for total loss of 5mC in some species.","PeriodicalId":501108,"journal":{"name":"bioRxiv - Molecular Biology","volume":"16 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142253420","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

HIV Vpr activates a nucleolar-specific ATR pathway to degrade the nucleolar stress sensor CCDC137 艾滋病毒Vpr激活核小体特异性ATR通路，降解核小体应激传感器CCDC137

bioRxiv - Molecular Biology Pub Date : 2024-09-13 DOI: 10.1101/2024.09.11.612530

Karly A Nisson, Rishi S Patel, Yennifer Delgado, Mehdi Bouhaddou, Lucie Etienne, Oliver I Fregoso

{"title":"HIV Vpr activates a nucleolar-specific ATR pathway to degrade the nucleolar stress sensor CCDC137","authors":"Karly A Nisson, Rishi S Patel, Yennifer Delgado, Mehdi Bouhaddou, Lucie Etienne, Oliver I Fregoso","doi":"10.1101/2024.09.11.612530","DOIUrl":"https://doi.org/10.1101/2024.09.11.612530","url":null,"abstract":"The lentiviral accessory protein Vpr engages an extensive network of cellular pathways to drive diverse host consequences. Of its many phenotypes, CRL4A-E3 ubiquitin ligase complex co-option, DNA damage response (DDR) engagement, and G2/M arrest are conserved and thus proposed to be functionally important. How Vpr effects these functions and whether they explain how Vpr dysregulates additional cellular pathways remain unclear. Here we leverage the ability of Vpr to deplete the nucleolar protein CCDC137 to understand how Vpr-induced DDR activation impacts nucleolar processes. We characterize CCDC137 as an indirect Vpr target whose degradation does not correlate with Vpr-induced G2/M arrest. Yet, degradation is conserved among Vpr from the pandemic HIV-1 and related SIVcpz/SIVgor, and it is triggered by genomic insults that activate a nucleolar ATR pathway in a manner similar to camptothecin. We determine that Vpr causes ATR-dependent features of nucleolar stress that correlate with CCDC137 degradation, including redistribution of nucleolar proteins, altered nucleolar morphology, and repressed ribosome biogenesis. Together, this data distinguishes CCDC137 as a non-canonical Vpr target that may serve as a sensor of nucleolar disruption, and in doing so, identifies a novel role for Vpr in nucleolar stress.","PeriodicalId":501108,"journal":{"name":"bioRxiv - Molecular Biology","volume":"22 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142212718","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Condensin loop extrusion properties, roadblocks, and role in homology search in S. cerevisiae 凝结蛋白环挤压特性、路障以及在 S. cerevisiae 同源搜索中的作用

bioRxiv - Molecular Biology Pub Date : 2024-09-13 DOI: 10.1101/2024.09.12.612585

Vinciane Piveteau, Hossein Salari, Agnes Dumont, Jerome Savocco, Chloe Dupont, Daniel Jost, Aurele Piazza

{"title":"Condensin loop extrusion properties, roadblocks, and role in homology search in S. cerevisiae","authors":"Vinciane Piveteau, Hossein Salari, Agnes Dumont, Jerome Savocco, Chloe Dupont, Daniel Jost, Aurele Piazza","doi":"10.1101/2024.09.12.612585","DOIUrl":"https://doi.org/10.1101/2024.09.12.612585","url":null,"abstract":"The in vivo mechanism, regulations by cis-acting roadblocks, and biological functions of loop extrusion by eukaryotic SMC complexes are incompletely defined. Here, using Hi-C, we identified two condensin-dependent contact stripes at the Recombination Enhancer (RE) and the rDNA in S. cerevisiae. We show that oriented, unidirectional loop extrusion proceeds from these sites with an estimated processivity ~170 kb and a density ~0.04-0.18 that varies across the cell cycle. Centromeres and highly-transcribed RNA PolII-dependent genes are permeable condensin roadblocks. Other positionally labile elements such as replication forks and Smc5/6 complexes bound to substrates generated in the absence of Top2 also hinder loop extrusion by condensin. Cohesin is not an obstacle for condensin. Finally, a DNA double-strand break at MAT blocks condensin, which results in the rapid establishment of a long-range RE-MAT loop that juxtaposes the recombination machinery with its HMLα donor target. Hence, all budding yeast SMCs are involved in recombinational DNA repair. We propose a revised model for donor selection during MAT switching that exploits specific properties of loop extrusion by condensin. It can serve as a paradigm for the establishment of other types of selective interactions along chromosomes.","PeriodicalId":501108,"journal":{"name":"bioRxiv - Molecular Biology","volume":"19 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142253423","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

53BP1 deficiency leads to hyperrecombination using break-induced replication (BIR) 53BP1 缺乏会导致断裂诱导复制（BIR）的过度重组

bioRxiv - Molecular Biology Pub Date : 2024-09-13 DOI: 10.1101/2024.09.11.612483

Sameer Bikram Shah, Youhang Li, Shibo Li, Qing Hu, Tong Wu, Yanmeng Shi, Tran Nguyen, Isaac Ive, Linda Shi, Hailong Wang, Xiaohua Wu

{"title":"53BP1 deficiency leads to hyperrecombination using break-induced replication (BIR)","authors":"Sameer Bikram Shah, Youhang Li, Shibo Li, Qing Hu, Tong Wu, Yanmeng Shi, Tran Nguyen, Isaac Ive, Linda Shi, Hailong Wang, Xiaohua Wu","doi":"10.1101/2024.09.11.612483","DOIUrl":"https://doi.org/10.1101/2024.09.11.612483","url":null,"abstract":"Break-induced replication (BIR) is mutagenic, and thus its use requires tight regulation, yet the underlying mechanisms remain elusive. Here we uncover an important role of 53BP1 in suppressing BIR after end resection at double strand breaks (DSBs), distinct from its end protection activity, providing insight into the mechanisms governing BIR regulation and DSB repair pathway selection. We demonstrate that loss of 53BP1 induces BIR-like hyperrecombination, in a manner dependent on Polα-primase-mediated end fill-in DNA synthesis on single-stranded DNA (ssDNA) overhangs at DSBs, leading to PCNA ubiquitination and PIF1 recruitment to activate BIR. On broken replication forks, where BIR is required for repairing single-ended DSBs (seDSBs), SMARCAD1 displaces 53BP1 to facilitate the localization of ubiquitinated PCNA and PIF1 to DSBs for BIR activation. Hyper BIR associated with 53BP1 deficiency manifests template switching and large deletions, underscoring another aspect of 53BP1 in suppressing genome instability. The synthetic lethal interaction between the 53BP1 and BIR pathways provides opportunities for targeted cancer treatment.","PeriodicalId":501108,"journal":{"name":"bioRxiv - Molecular Biology","volume":"12 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142253422","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Synergistic DNA and RNA binding of the Hox transcription factor Ultrabithorax coordinates splicing and shapes in vivo homeotic functions Hox转录因子Ultrabithorax与DNA和RNA的协同结合可协调剪接并塑造体内同源功能

bioRxiv - Molecular Biology Pub Date : 2024-09-12 DOI: 10.1101/2024.09.10.612310

Constanza Blanco, Wan Xiang, Panagiotis Boumpas, Maily Scorcelletti, Ashley Suraj Hermon, Jiemin Wong, Samir Merabet, Julie Carnesecchi

{"title":"Synergistic DNA and RNA binding of the Hox transcription factor Ultrabithorax coordinates splicing and shapes in vivo homeotic functions","authors":"Constanza Blanco, Wan Xiang, Panagiotis Boumpas, Maily Scorcelletti, Ashley Suraj Hermon, Jiemin Wong, Samir Merabet, Julie Carnesecchi","doi":"10.1101/2024.09.10.612310","DOIUrl":"https://doi.org/10.1101/2024.09.10.612310","url":null,"abstract":"The dual interaction of many transcription factors (TFs) with both DNA and RNA is an underexplored issue that could fundamentally reshape our understanding of gene regulation. We address this central issue by investigating the RNA binding activity of the Drosophila Hox TF Ultrabithorax (Ubx) in alternative splicing and morphogenesis. Relying on molecular and genetic interactions, we uncover a homodimerization-dependent mechanism by which Ubx regulates splicing. Notably, this mechanism enables the decoupling of Ubx-DNA and -RNA binding activity in splicing. We identify a critical residue for Ubx-RNA binding and demonstrate the essential role of Ubx-RNA binding ability for its homeotic functions. Overall, we uncover a unique mechanism for Ubx-mediated splicing and underscore the critical contribution of synergistic DNA/RNA binding for its morphogenetic functions. These findings advance our understanding of co-transcriptional regulation and highlight the significance of TF-DNA/RNA synergistic function in shaping gene regulatory networks in living organisms.","PeriodicalId":501108,"journal":{"name":"bioRxiv - Molecular Biology","volume":"33 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142212719","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Screening of histone mutants reveals a domain within the N-terminal tail of histone H3 that regulates the Tup1-independent repressive role of Cyc8 at the active FLO1 对组蛋白突变体的筛选揭示了组蛋白 H3 N 端尾部的一个结构域，该结构域可调节 Cyc8 在活性 FLO1 上发挥与 Tup1 无关的抑制作用

bioRxiv - Molecular Biology Pub Date : 2024-09-12 DOI: 10.1101/2024.09.10.612373

Ranu Singh, Raghuvir Singh Tomar

{"title":"Screening of histone mutants reveals a domain within the N-terminal tail of histone H3 that regulates the Tup1-independent repressive role of Cyc8 at the active FLO1","authors":"Ranu Singh, Raghuvir Singh Tomar","doi":"10.1101/2024.09.10.612373","DOIUrl":"https://doi.org/10.1101/2024.09.10.612373","url":null,"abstract":"Yeast flocculation relies on cell surface flocculin proteins encoded by the FLO1 gene. The expression of FLO1 is antagonistically regulated by the Tup1-Cyc8 and the Swi-Snf complexes. The Post translational modifications of core histones regulate the transcription of Tup1-Cyc8-regulated genes. However, the mechanisms by which the physical presence of tail residues regulate FLO1 transcription process and flocculation is yet to be completely understood. Through screening we have identified a new region within the N-terminal tail of histone H3 regulating the transcription of FLO1 and FLO5. One of the histone H3 N-terminal truncation mutants H3del(17 to 24) showed higher FLO1 expression compared to wild type H3. Results revealed that in absence of 17 to 24 stretch the occupancy of Cyc8 decreases from the upstream regions of FLO1. Additionally, analysis suggests that Hda1 is required for the Cyc8-mediated repression of FLO1. Altogether we demonstrate that 17 to 24 stretch is essential for the Tup1 independent binding of Cyc8 at the promoters assisted by Hda1, leading to the strong repression of FLO1 transcription. In the absence of the 17 to 24 stretch, Cyc8 cannot bind, resulting in uncontrolled transcription of FLO1.","PeriodicalId":501108,"journal":{"name":"bioRxiv - Molecular Biology","volume":"25 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142212720","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0