Current GeneticsPub Date : 2021-08-01Epub Date: 2021-03-12DOI: 10.1007/s00294-021-01166-3
Richard Cardoso da Silva, Gerben Vader
{"title":"Getting there: understanding the chromosomal recruitment of the AAA+ ATPase Pch2/TRIP13 during meiosis.","authors":"Richard Cardoso da Silva, Gerben Vader","doi":"10.1007/s00294-021-01166-3","DOIUrl":"https://doi.org/10.1007/s00294-021-01166-3","url":null,"abstract":"<p><p>The generally conserved AAA+ ATPase Pch2/TRIP13 is involved in diverse aspects of meiosis, such as prophase checkpoint function, DNA break regulation, and meiotic recombination. The controlled recruitment of Pch2 to meiotic chromosomes allows it to use its ATPase activity to influence HORMA protein-dependent signaling. Because of the connection between Pch2 chromosomal recruitment and its functional roles in meiosis, it is important to reveal the molecular details that govern Pch2 localization. Here, we review the current understanding of the different factors that control the recruitment of Pch2 to meiotic chromosomes, with a focus on research performed in budding yeast. During meiosis in this organism, Pch2 is enriched within the nucleolus, where it likely associates with the specialized chromatin of the ribosomal (r)DNA. Pch2 is also found on non-rDNA euchromatin, where its recruitment is contingent on Zip1, a component of the synaptonemal complex (SC) that assembles between homologous chromosomes. We discuss recent findings connecting the recruitment of Pch2 with its association with the Origin Recognition Complex (ORC) and reliance on RNA Polymerase II-dependent transcription. In total, we provide a comprehensive overview of the pathways that control the chromosomal association of an important meiotic regulator.</p>","PeriodicalId":10918,"journal":{"name":"Current Genetics","volume":"67 4","pages":"553-565"},"PeriodicalIF":2.5,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00294-021-01166-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25470681","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Current GeneticsPub Date : 2021-08-01Epub Date: 2021-03-19DOI: 10.1007/s00294-021-01178-z
Kanchan Jaswal, Megha Shrivastava, Rachna Chaba
{"title":"Revisiting long-chain fatty acid metabolism in Escherichia coli: integration with stress responses.","authors":"Kanchan Jaswal, Megha Shrivastava, Rachna Chaba","doi":"10.1007/s00294-021-01178-z","DOIUrl":"https://doi.org/10.1007/s00294-021-01178-z","url":null,"abstract":"<p><p>Long-chain fatty acids (LCFAs) are a tremendous source of metabolic energy, an essential component of membranes, and important effector molecules that regulate a myriad of cellular processes. As an energy-rich nutrient source, the role of LCFAs in promoting bacterial survival and infectivity is well appreciated. LCFA degradation generates a large number of reduced cofactors that may confer redox stress; therefore, it is imperative to understand how bacteria deal with this paradoxical situation. Although the LCFA utilization pathway has been studied in great detail, especially in Escherichia coli, where the earliest studies date back to the 1960s, the interconnection of LCFA degradation with bacterial stress responses remained largely unexplored. Recent work in E. coli shows that LCFA degradation induces oxidative stress and also impedes oxidative protein folding. Importantly, both issues arise due to the insufficiency of ubiquinone, a lipid-soluble electron carrier in the electron transport chain. However, to maintain redox homeostasis, bacteria induce sophisticated cellular responses. Here, we review these findings in light of our current knowledge of the LCFA metabolic pathway, metabolism-induced oxidative stress, the process of oxidative protein folding, and stress combat mechanisms. We discuss probable mechanisms for the activation of defense players during LCFA metabolism and the likely feedback imparted by them. We suggest that besides defending against intrinsic stresses, LCFA-mediated upregulation of stress response pathways primes bacteria to adapt to harsh external environments. Collectively, the interplay between LCFA metabolism and stress responses is likely an important factor that underlies the success of LCFA-utilizing bacteria in the host.</p>","PeriodicalId":10918,"journal":{"name":"Current Genetics","volume":"67 4","pages":"573-582"},"PeriodicalIF":2.5,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00294-021-01178-z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25495123","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Current GeneticsPub Date : 2021-08-01Epub Date: 2021-03-18DOI: 10.1007/s00294-021-01169-0
Mathieu Hénault
{"title":"The challenges of predicting transposable element activity in hybrids.","authors":"Mathieu Hénault","doi":"10.1007/s00294-021-01169-0","DOIUrl":"https://doi.org/10.1007/s00294-021-01169-0","url":null,"abstract":"<p><p>Transposable elements (TEs) are ubiquitous mobile genetic elements that hold both disruptive and adaptive potential for species. It has long been postulated that their activity may be triggered by hybridization, a hypothesis that received mixed support from studies in various species. While host defense mechanisms against TEs are being elucidated, the increasing volume of genomic data and bioinformatic tools specialized in TE detection enable in-depth characterization of TEs at the levels of species and populations. Here, I borrow elements from the genome ecology theory to illustrate how knowledge of the diversity of TEs and host defense mechanisms may help predict the activity of TEs in the face of hybridization, and how current limitations make this task especially challenging.</p>","PeriodicalId":10918,"journal":{"name":"Current Genetics","volume":"67 4","pages":"567-572"},"PeriodicalIF":2.5,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00294-021-01169-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25495393","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Current GeneticsPub Date : 2021-08-01Epub Date: 2021-03-08DOI: 10.1007/s00294-021-01163-6
Joo-Yeon Lim, Seung-Hyun Jang, Hee-Moon Park
{"title":"Mannitol-1-phosphate dehydrogenase, MpdA, is required for mannitol production in vegetative cells and involved in hyphal branching, heat resistance of conidia and sexual development in Aspergillus nidulans.","authors":"Joo-Yeon Lim, Seung-Hyun Jang, Hee-Moon Park","doi":"10.1007/s00294-021-01163-6","DOIUrl":"https://doi.org/10.1007/s00294-021-01163-6","url":null,"abstract":"<p><p>Aspergillus nidulans produces cleistothecia as sexual reproductive organs in a process affected by genetic and external factors. To gain a deeper insight into A. nidulans sexual development, we performed comparative proteome analyses based on the wild type developmental periods. We identified sexual development-specific proteins with a more than twofold increase in production during hypoxia or the sexual period compared to the asexual period. Among the sexual development-specific proteins analyzed by gene-deletion experiments and functional assays, MpdA, a putative mannitol-1-phosphate 5-dehydrogenase, plays multiple roles in growth and differentiation of A. nidulans. The most distinct mpdA-deletion phenotype was ascosporogenesis failure. Genetic mpdA deletion resulted in small cleistothecia with no functional ascospores. Transcriptional analyses indicated that MpdA modulates the expression of key development- and meiosis-regulatory genes during sexual development. The mpdA deletion increased hyphal branching and decreased conidial heat resistance. Mannitol production in conidia showed no difference, whereas it was decreased in mycelia and sexual cultures. Addition of mannitol during vegetative growth recovered the defects in conidial heat resistance and ascospore genesis. Taken together, these results indicate that MpdA plays an important role in sexual development, hyphal branching, and conidial heat resistance in Aspergillus nidulans.</p>","PeriodicalId":10918,"journal":{"name":"Current Genetics","volume":"67 4","pages":"613-630"},"PeriodicalIF":2.5,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00294-021-01163-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25448879","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Human OVCA2 and its homolog FSH3-induced apoptosis in Saccharomyces cerevisiae.","authors":"Ramachandran Gowsalya, Chidambaram Ravi, Vasanthi Nachiappan","doi":"10.1007/s00294-021-01171-6","DOIUrl":"https://doi.org/10.1007/s00294-021-01171-6","url":null,"abstract":"<p><p>Mammalian ovarian tumor suppressor candidate 2 (OVCA2) gene belongs to the family of serine hydrolase (FSH). This study aimed to elucidate the functional similarities of OVCA2 with its yeast homolog genes (FSH1, FSH2, and FSH3) regarding apoptosis. We found that the expression of OVCA2 in Saccharomyces cerevisiae increased production of reactive oxygen species (ROS), decreased cell growth, disturbed mitochondrial morphology, reduced membrane potential, increased chromatin condensation, and externalization of phosphatidylserine (PS) (annexin V/propidium iodide staining) indicating induced apoptotic cell death in yeast. We also showed that complementation of OVCA2 in fsh3Δ cells reduced cell growth and increased the apoptotic phenotypes. Collectively, our results suggest that complementation of human OVCA2 in fsh3Δ cells induced apoptosis in S. cerevisiae.</p>","PeriodicalId":10918,"journal":{"name":"Current Genetics","volume":"67 4","pages":"631-640"},"PeriodicalIF":2.5,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00294-021-01171-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25484712","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Two homologs of the Cat8 transcription factor are involved in the regulation of ethanol utilization in Komagataella phaffii.","authors":"Diane Barbay, Monika Mačáková, Leander Sützl, Sonakshi De, Diethard Mattanovich, Brigitte Gasser","doi":"10.1007/s00294-021-01165-4","DOIUrl":"https://doi.org/10.1007/s00294-021-01165-4","url":null,"abstract":"<p><p>The transcription factors Cat8 and Sip4 were described in Saccharomyces cerevisiae and Kluyveromyces lactis to have very similar DNA binding domains and to be necessary for derepression of a variety of genes under non-fermentative growth conditions via binding to the carbon source responsive elements (CSREs). The methylotrophic yeast Komagataella phaffii (syn Pichia pastoris) has two transcription factors (TFs), which are putative homologs of Cat8 based on sequence similarity, termed Cat8-1 and Cat8-2. It is yet unclear in which cellular processes they are involved and if one of them is actually the homolog of Sip4. To study the roles of the Cat8 homologs in K. phaffii, overexpression or deletion strains were generated for the two TFs. The ability of these mutant strains to grow on different carbon sources was tested, and transcript levels of selected genes from the carbon metabolism were quantified. Our experiments showed that the TFs are required for the growth of K. phaffii on C2 carbon sources, but not on glucose, glycerol or methanol. K. phaffii deleted for Cat8-1 showed impaired growth on acetate, while both Cat8-1 and Cat8-2 are involved in the growth of K. phaffii on ethanol. Correspondingly, both TFs are participating in the activation of ADH2, ALD4 and ACS1, three genes encoding enzymes important for the assimilation of ethanol. Different from S. cerevisiae and K. lactis, Cat8-1 is not regulating the transcription of the putative Sip4-family member Cat8-2 in K. phaffii. Furthermore, Cat8-1 is necessary for the activation of genes from the glyoxylate cycle, whereas Cat8-2 is necessary for the activation of genes from the carnitine shuttle. Neither Cat8-1 nor Cat8-2 are required for the activation of gluconeogenesis genes. Finally, the CAT8-2 gene is repressed by the Mig1-2 transcription factor on glucose and autorepressed by the Cat8-2 protein on all tested carbon sources. Our study identified the involvement of K. phaffii Cat8-1 and Cat8-2 in C2-metabolism, and highlighted similarities and differences to their homologs in other yeast species.</p>","PeriodicalId":10918,"journal":{"name":"Current Genetics","volume":"67 4","pages":"641-661"},"PeriodicalIF":2.5,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00294-021-01165-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25483068","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Current GeneticsPub Date : 2021-08-01Epub Date: 2021-03-14DOI: 10.1007/s00294-021-01175-2
Lihi Gershon, Martin Kupiec
{"title":"Histones on fire: the effect of Dun1 and Mrc1 on origin firing and replication of hyper-acetylated genomes.","authors":"Lihi Gershon, Martin Kupiec","doi":"10.1007/s00294-021-01175-2","DOIUrl":"https://doi.org/10.1007/s00294-021-01175-2","url":null,"abstract":"<p><p>As cells replicate their DNA, there is a need to synthesize new histones with which to wrap it. Newly synthesized H3 histones that are incorporated into the assembling chromatin behind the replication fork are acetylated at lysine 56. The acetylation is removed by two deacetylases, Hst3 and Hst4. This process is tightly regulated and any perturbation leads to genomic instability and replicative stress. We recently showed that Dun1, a kinase implicated mainly in the regulation of dNTPs, is vital in cells with hyper-acetylation, to counteract Rad53's inhibition on late-firing origins of replication. Our work showed that ∆hst3 ∆hst4 cells depend on late origin firing for survival, and are unable to prevent Rad53's inhibition when Dun1 is inactive. Thus, our work describes a role for Dun1 that is independent on its known function as a regulator of dNTP levels. Here we show that Mrc1 (Claspin in mammals), a protein that moves with the replicating fork and participates in both replication and checkpoint functions, plays also an essential role in the absence of H3K56Ac deacetylation. The sum of the results shown here and in our recent publication suggests that dormant origins are also utilized in these cells, making Mrc1, which regulates firing from these origins, also essential when histone H3 is hyper-acetylated. Thus, cells suffering from hyper-acetylation of H3K56 experience replication stress caused by a combination of prone-to-collapse forks and limited replication tracts. This combination makes both Dun1 and Mrc1, each acting on different targets, essential for viability.</p>","PeriodicalId":10918,"journal":{"name":"Current Genetics","volume":"67 4","pages":"501-510"},"PeriodicalIF":2.5,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00294-021-01175-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25472780","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Current GeneticsPub Date : 2021-08-01Epub Date: 2021-03-21DOI: 10.1007/s00294-021-01174-3
Jingxun Chen, Elçin Ünal
{"title":"Meiotic regulation of the Ndc80 complex composition and function.","authors":"Jingxun Chen, Elçin Ünal","doi":"10.1007/s00294-021-01174-3","DOIUrl":"https://doi.org/10.1007/s00294-021-01174-3","url":null,"abstract":"<p><p>This review describes the current models for how the subunit abundance of the Ndc80 complex, a key kinetochore component, is regulated in budding yeast and metazoan meiosis. The past decades of kinetochore research have established the Ndc80 complex to be a key microtubule interactor and a central hub for regulating chromosome segregation. Recent studies further demonstrate that Ndc80 is the limiting kinetochore subunit that dictates the timing of kinetochore activation in budding yeast meiosis. Here, we discuss the molecular circuits that regulate Ndc80 protein synthesis and degradation in budding yeast meiosis and compare the findings with those from metazoans. We envision the regulatory principles discovered in budding yeast to be conserved in metazoans, thereby providing guidance into future investigations on kinetochore regulation in human health and disease.</p>","PeriodicalId":10918,"journal":{"name":"Current Genetics","volume":"67 4","pages":"511-518"},"PeriodicalIF":2.5,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00294-021-01174-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25499108","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Current GeneticsPub Date : 2021-08-01Epub Date: 2021-02-28DOI: 10.1007/s00294-021-01167-2
Meng Ye, Hang Jiang, Xianhui Fu, Jin-Rong Xu, Cong Jiang
{"title":"Fng1 is involved in crosstalk between histone acetylation and methylation.","authors":"Meng Ye, Hang Jiang, Xianhui Fu, Jin-Rong Xu, Cong Jiang","doi":"10.1007/s00294-021-01167-2","DOIUrl":"https://doi.org/10.1007/s00294-021-01167-2","url":null,"abstract":"<p><p>The histone modifications usually form complicated networks to regulate accessibility of DNA and transcription. Identification of proteins that are involved in the crosstalk among different histone modifications will help to better understand the epigenetic regulatory network in eukaryotes. The Inhibitor of Growth (ING) proteins represent a tumor suppressor family were first linked to histone modification in yeast and their functions in epigenetic regulation were further characterized. This review summarizes the crosstalk of histone modification in fungi and describes recently achieved mechanistic insights into the role of Fng1 (an ING protein in filamentous ascomycetes) in this process. We conclude that Fng1 is involved in crosstalk among histone acetylation, deacetylation and methylation.</p>","PeriodicalId":10918,"journal":{"name":"Current Genetics","volume":"67 4","pages":"535-538"},"PeriodicalIF":2.5,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s00294-021-01167-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25418931","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}