Different Roles for Aurora B in Condensin Targeting During Mitosis and Meiosis
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Dynamic Molecular Linkers of the Genome: the First Decade of SMC Proteins
Downloaded from genesdev.cshlp.org on October 8, 2021 - Published by Cold Spring Harbor Laboratory Press REVIEW Dynamic molecular linkers of the genome: the first decade of SMC proteins Ana Losada1 and Tatsuya Hirano2,3 1Spanish National Cancer Center (CNIO), Madrid E-28029, Spain; 2Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA Structural maintenance of chromosomes (SMC) proteins in eukaryotes. The proposed actions of cohesin and con- are chromosomal ATPases, highly conserved from bac- densins offer a plausible, if not complete, explanation for teria to humans, that play fundamental roles in many the sudden appearance of thread-like “substances” (the aspects of higher-order chromosome organization and chromosomes) and their longitudinal splitting during dynamics. In eukaryotes, SMC1 and SMC3 act as the mitosis, first described by Walther Flemming (1882). core of the cohesin complexes that mediate sister chro- Remarkably, SMC proteins are conserved among the matid cohesion, whereas SMC2 and SMC4 function as three phyla of life, indicating that the basic strategy of the core of the condensin complexes that are essential chromosome organization may be evolutionarily con- for chromosome assembly and segregation. Another served from bacteria to humans. An emerging theme is complex containing SMC5 and SMC6 is implicated in that SMC proteins are dynamic molecular linkers of the DNA repair and checkpoint responses. The SMC com- genome that actively fold, tether, and manipulate DNA plexes form unique ring- or V-shaped structures with strands. Their diverse functions range far beyond chro- long coiled-coil arms, and function as ATP-modulated, mosome segregation, and involve nearly all aspects of dynamic molecular linkers of the genome. -
Building the Interphase Nucleus: a Study on the Kinetics of 3D Chromosome Formation, Temporal Relation to Active Transcription, and the Role of Nuclear Rnas
University of Massachusetts Medical School eScholarship@UMMS GSBS Dissertations and Theses Graduate School of Biomedical Sciences 2020-07-28 Building the Interphase Nucleus: A study on the kinetics of 3D chromosome formation, temporal relation to active transcription, and the role of nuclear RNAs Kristin N. Abramo University of Massachusetts Medical School Let us know how access to this document benefits ou.y Follow this and additional works at: https://escholarship.umassmed.edu/gsbs_diss Part of the Bioinformatics Commons, Cell Biology Commons, Computational Biology Commons, Genomics Commons, Laboratory and Basic Science Research Commons, Molecular Biology Commons, Molecular Genetics Commons, and the Systems Biology Commons Repository Citation Abramo KN. (2020). Building the Interphase Nucleus: A study on the kinetics of 3D chromosome formation, temporal relation to active transcription, and the role of nuclear RNAs. GSBS Dissertations and Theses. https://doi.org/10.13028/a9gd-gw44. Retrieved from https://escholarship.umassmed.edu/ gsbs_diss/1099 Creative Commons License This work is licensed under a Creative Commons Attribution-Noncommercial 4.0 License This material is brought to you by eScholarship@UMMS. It has been accepted for inclusion in GSBS Dissertations and Theses by an authorized administrator of eScholarship@UMMS. For more information, please contact [email protected]. BUILDING THE INTERPHASE NUCLEUS: A STUDY ON THE KINETICS OF 3D CHROMOSOME FORMATION, TEMPORAL RELATION TO ACTIVE TRANSCRIPTION, AND THE ROLE OF NUCLEAR RNAS A Dissertation Presented By KRISTIN N. ABRAMO Submitted to the Faculty of the University of Massachusetts Graduate School of Biomedical Sciences, Worcester in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSPOPHY July 28, 2020 Program in Systems Biology, Interdisciplinary Graduate Program BUILDING THE INTERPHASE NUCLEUS: A STUDY ON THE KINETICS OF 3D CHROMOSOME FORMATION, TEMPORAL RELATION TO ACTIVE TRANSCRIPTION, AND THE ROLE OF NUCLEAR RNAS A Dissertation Presented By KRISTIN N. -
Understanding Molecular Functions of the SMC5/6 Complex
G C A T T A C G G C A T genes Review Scaffolding for Repair: Understanding Molecular Functions of the SMC5/6 Complex Mariana Diaz 1,2 and Ales Pecinka 1,* ID 1 Institute of Experimental Botany of the Czech Academy of Sciences (IEB), Centre of the Region Haná for Biotechnological and Agricultural Research, Šlechtitelu˚ 31, 77900 Olomouc-Holice, Czech Republic 2 Max Planck Institute for Plant Breeding Research (MPIPZ), Carl-von-Linné-Weg 10, 50829 Cologne, Germany; [email protected] * Correspondence: [email protected]; Tel.: +420-585-238-709 Received: 15 November 2017; Accepted: 4 January 2018; Published: 12 January 2018 Abstract: Chromosome organization, dynamics and stability are required for successful passage through cellular generations and transmission of genetic information to offspring. The key components involved are Structural maintenance of chromosomes (SMC) complexes. Cohesin complex ensures proper chromatid alignment, condensin complex chromosome condensation and the SMC5/6 complex is specialized in the maintenance of genome stability. Here we summarize recent knowledge on the composition and molecular functions of SMC5/6 complex. SMC5/6 complex was originally identified based on the sensitivity of its mutants to genotoxic stress but there is increasing number of studies demonstrating its roles in the control of DNA replication, sister chromatid resolution and genomic location-dependent promotion or suppression of homologous recombination. Some of these functions appear to be due to a very dynamic interaction with cohesin or other repair complexes. Studies in Arabidopsis indicate that, besides its canonical function in repair of damaged DNA, the SMC5/6 complex plays important roles in regulating plant development, abiotic stress responses, suppression of autoimmune responses and sexual reproduction. -
Nuclear Domains
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Cold Spring Harbor Laboratory Institutional Repository CELL SCIENCE AT A GLANCE 2891 Nuclear domains dynamic structures and, in addition, nuclear pore complex has been shown to rapid protein exchange occurs between have a remarkable substructure, in which David L. Spector many of the domains and the a basket extends into the nucleoplasm. Cold Spring Harbor Laboratory, One Bungtown nucleoplasm (Misteli, 2001). An The peripheral nuclear lamina lies Road, Cold Spring Harbor, NY 11724, USA extensive effort is currently underway by inside the nuclear envelope and is (e-mail: [email protected]) numerous laboratories to determine the composed of lamins A/C and B and is biological function(s) associated with thought to play a role in regulating Journal of Cell Science 114, 2891-2893 (2001) © The Company of Biologists Ltd each domain. The accompanying poster nuclear envelope structure and presents an overview of commonly anchoring interphase chromatin at the The mammalian cell nucleus is a observed nuclear domains. nuclear periphery. Internal patches of membrane-bound organelle that contains lamin protein are also present in the the machinery essential for gene The nucleus is bounded by a nuclear nucleoplasm (Moir et al., 2000). The expression. Although early studies envelope, a double-membrane structure, cartoon depicts much of the nuclear suggested that little organization exists of which the outer membrane is envelope/peripheral lamina as within this compartment, more contiguous with the rough endoplasmic transparent, so that internal structures contemporary studies have identified an reticulum and is often studded with can be more easily observed. -
DEAD-Box RNA Helicases in Cell Cycle Control and Clinical Therapy
cells Review DEAD-Box RNA Helicases in Cell Cycle Control and Clinical Therapy Lu Zhang 1,2 and Xiaogang Li 2,3,* 1 Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China; [email protected] 2 Department of Internal Medicine, Mayo Clinic, 200 1st Street, SW, Rochester, MN 55905, USA 3 Department of Biochemistry and Molecular Biology, Mayo Clinic, 200 1st Street, SW, Rochester, MN 55905, USA * Correspondence: [email protected]; Tel.: +1-507-266-0110 Abstract: Cell cycle is regulated through numerous signaling pathways that determine whether cells will proliferate, remain quiescent, arrest, or undergo apoptosis. Abnormal cell cycle regula- tion has been linked to many diseases. Thus, there is an urgent need to understand the diverse molecular mechanisms of how the cell cycle is controlled. RNA helicases constitute a large family of proteins with functions in all aspects of RNA metabolism, including unwinding or annealing of RNA molecules to regulate pre-mRNA, rRNA and miRNA processing, clamping protein complexes on RNA, or remodeling ribonucleoprotein complexes, to regulate gene expression. RNA helicases also regulate the activity of specific proteins through direct interaction. Abnormal expression of RNA helicases has been associated with different diseases, including cancer, neurological disorders, aging, and autosomal dominant polycystic kidney disease (ADPKD) via regulation of a diverse range of cellular processes such as cell proliferation, cell cycle arrest, and apoptosis. Recent studies showed that RNA helicases participate in the regulation of the cell cycle progression at each cell cycle phase, including G1-S transition, S phase, G2-M transition, mitosis, and cytokinesis. -
Multiple Controls Regulate Nucleostemin Partitioning Between Nucleolus and Nucleoplasm
5124 Research Article Multiple controls regulate nucleostemin partitioning between nucleolus and nucleoplasm Lingjun Meng1, Hiroaki Yasumoto1 and Robert Y. L. Tsai1,* 1Center for Cancer and Stem Cell Biology, Alkek Institute of Biosciences and Technology, Texas A&M Health Science Center, 2121 W Holcombe Blvd, Houston, TX 77030-3303, USA *Author for correspondence (e-mail: [email protected]) Accepted 6 October 2006 Journal of Cell Science 119, 5124-5136 Published by The Company of Biologists 2006 doi:10.1242/jcs.03292 Summary Nucleostemin plays an essential role in maintaining the nucleostemin. It interacts with both the basic and the GTP- continuous proliferation of stem cells and cancer cells. The binding domains of nucleostemin through a non-nucleolus- movement of nucleostemin between the nucleolus and the targeting region. Overexpression of the nucleolus-targeting nucleoplasm provides a dynamic way to partition the domain of RSL1D1 alone disperses nucleolar nucleostemin. nucleostemin protein between these two compartments. Loss of RSL1D1 expression reduces the compartmental size Here, we show that nucleostemin contains two nucleolus- and amount of nucleostemin in the nucleolus. Our work targeting regions, the basic and the GTP-binding domains, reveals that the partitioning of nucleostemin employs that exhibit a short and a long nucleolar retention time, complex mechanisms involving both nucleolar and respectively. In a GTP-unbound state, the nucleolus- nucleoplasmic components, and provides insight into the targeting activity of nucleostemin is blocked by a post-translational regulation of its activity. mechanism that traps its intermediate domain in the nucleoplasm. A nucleostemin-interacting protein, RSL1D1, Supplementary material available online at was identified that contains a ribosomal L1-domain. -
Cytochemical Features Common to Nucleoli and Cytoplasmic Nucleoloids of Olea Europaea Meiocytes: Detection of Rrna by in Situ Hybridization
Journal of Cell Science 107, 621-629 (1994) 621 Printed in Great Britain © The Company of Biologists Limited 1994 JCS8341 Cytochemical features common to nucleoli and cytoplasmic nucleoloids of Olea europaea meiocytes: detection of rRNA by in situ hybridization J. D. Alché, M. C. Fernández and M. I. Rodríguez-García* Plant Biochemistry, Molecular and Cellular Biology Department, Estación Experimental del Zaidín, CSIC, Profesor Albareda 1, E- 18008 Granada, Spain *Author for correspondence SUMMARY We used light and electron microscopic techniques to study highly phosphorylated proteins. Immunohistochemical the composition of cytoplasmic nucleoloids during meiotic techniques failed to detect DNA in either structure. In situ division in Olea europaea. Nucleoloids were found in two hybridization to a 18 S rRNA probe demonstrated the clearly distinguishable morphological varieties: one similar presence of ribosomal transcripts in both the nucleolus and in morphology to the nucleolus, and composed mainly of nucleoloids. These similarities in morphology and compo- dense fibrillar component, and another surrounded by sition may reflect similar functionalities. many ribosome-like particles. Cytochemical and immuno- cytochemical techniques showed similar reactivities in nucleoloids and the nucleolus: both are ribonucleoproteic Key words: nucleoloids, nucleolar proteins, rRNA, in situ in nature, and possess argyrophillic, argentaffinic and hybridization INTRODUCTION lentum (Carretero and Rodríguez-García, unpublished observa- tions). The reason for this diversity is unknown. Cytoplasmic bodies similar in morphology and ultrastructural Nucleoloids have rarely been studied in genera other than characteristics to the nucleolus have been reported many times Lilium. Cytoplasmic nucleoloids are very common in Olea in relation to plant meiosis (Latter, 1926; Frankel, 1937; europaea during microsporogenesis and their large size and Hakansson and Levan, 1942; Gavaudan, 1948; Lindemann, peculiar morphological characteristics make them a good 1956). -
Nucleolus: a Central Hub for Nuclear Functions Olga Iarovaia, Elizaveta Minina, Eugene Sheval, Daria Onichtchouk, Svetlana Dokudovskaya, Sergey Razin, Yegor Vassetzky
Nucleolus: A Central Hub for Nuclear Functions Olga Iarovaia, Elizaveta Minina, Eugene Sheval, Daria Onichtchouk, Svetlana Dokudovskaya, Sergey Razin, Yegor Vassetzky To cite this version: Olga Iarovaia, Elizaveta Minina, Eugene Sheval, Daria Onichtchouk, Svetlana Dokudovskaya, et al.. Nucleolus: A Central Hub for Nuclear Functions. Trends in Cell Biology, Elsevier, 2019, 29 (8), pp.647-659. 10.1016/j.tcb.2019.04.003. hal-02322927 HAL Id: hal-02322927 https://hal.archives-ouvertes.fr/hal-02322927 Submitted on 18 Nov 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Nucleolus: A Central Hub for Nuclear Functions Olga Iarovaia, Elizaveta Minina, Eugene Sheval, Daria Onichtchouk, Svetlana Dokudovskaya, Sergey Razin, Yegor Vassetzky To cite this version: Olga Iarovaia, Elizaveta Minina, Eugene Sheval, Daria Onichtchouk, Svetlana Dokudovskaya, et al.. Nucleolus: A Central Hub for Nuclear Functions. Trends in Cell Biology, Elsevier, 2019, 29 (8), pp.647-659. 10.1016/j.tcb.2019.04.003. hal-02322927 HAL Id: hal-02322927 https://hal.archives-ouvertes.fr/hal-02322927 Submitted on 18 Nov 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. -
Gemin4 Is an Essential Gene in Mice, and Its Overexpression in Human Cells Causes Relocalization of the SMN Complex to the Nucleoplasm Ingo D
© 2018. Published by The Company of Biologists Ltd | Biology Open (2018) 7, bio032409. doi:10.1242/bio.032409 RESEARCH ARTICLE Gemin4 is an essential gene in mice, and its overexpression in human cells causes relocalization of the SMN complex to the nucleoplasm Ingo D. Meier1,*,§, Michael P. Walker1,2,‡,§ and A. Gregory Matera¶ ABSTRACT nuclear ribonucleoproteins (snRNPs). Each of these snRNPs Gemin4 is a member of the Survival Motor Neuron (SMN) protein contains a common set of seven RNA binding factors, called Sm complex, which is responsible for the assembly and maturation of Sm- proteins, that forms a heptameric ring around the snRNA, known as class small nuclear ribonucleoproteins (snRNPs). In metazoa, Sm the Sm core. Biogenesis of the Sm core is carried out by another snRNPs are assembled in the cytoplasm and subsequently imported macromolecular assemblage called the Survival Motor Neuron into the nucleus. We previously showed that the SMN complex is (SMN) complex, consisting of at least nine proteins (Gemins 2-8, required for snRNP import in vitro, although it remains unclear which unrip and SMN) (reviewed in Battle et al., 2006a; Matera et al., specific components direct this process. Here, we report that Gemin4 2007; Matera and Wang, 2014). overexpression drives SMN and the other Gemin proteins from the Following RNA polymerase II-mediated transcription in the cytoplasm into the nucleus. Moreover, it disrupts the subnuclear nucleus, pre-snRNAs are exported to the cytoplasm for assembly localization of the Cajal body marker protein, coilin, in a dose- into stable RNP particles (Jarmolowski et al., 1994; Ohno et al., dependent manner. -
Paraspeckles
Downloaded from http://cshperspectives.cshlp.org/ on October 2, 2021 - Published by Cold Spring Harbor Laboratory Press Paraspeckles Archa H. Fox1 and Angus I. Lamond2 1Western Australian Institute for Medical Research and Centre For Medical Research, University of Western Australia, Crawley 6009 Western Australia, Australia 2Wellcome Trust Centre for Gene Regulation & Expression, College of Life Sciences, University of Dundee DUNDEE DD1 5EH UK Correspondence: [email protected] Paraspeckles are a relatively new class of subnuclear bodies found in the interchromatin space of mammalian cells. They are RNA-protein structures formed by the interaction between a long nonprotein-coding RNA species, NEAT1/Men 1/b, and members of the DBHS (Drosophila Behavior Human Splicing) family of proteins: P54NRB/NONO, PSPC1, and PSF/SFPQ. Paraspeckles are critical to the control of gene expression through the nuclear retention of RNA containing double-stranded RNA regions that have been subject to adenosine-to-inosine editing. Through this mechanism paraspeckles and their components may ultimately have a role in controlling gene expression during many cellular processes including differentiation, viral infection, and stress responses. DISCOVERY OF PARASPECKLES human nucleoli, 271 proteins were identified, he cell nucleus is a large and complex cellu- 30% of which were novel (Andersen et al. Tlar organelle with an intricate internal or- 2002). A follow up analysis on one of these ganization that is still not fully characterized. newly identified novel proteins, showed that it One feature of nuclear organization is the was not enriched in nucleoli, but instead was presence of distinct subnuclear bodies, each of found diffusely distributed within the nucleo- which contain specific nuclear proteins and plasm as well as concentrated in 5–20 sub- nucleic acids (Platani and Lamond 2004). -
1 the Nucleoporin ELYS Regulates Nuclear Size by Controlling NPC
bioRxiv preprint doi: https://doi.org/10.1101/510230; this version posted January 2, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. The nucleoporin ELYS regulates nuclear size by controlling NPC number and nuclear import capacity Predrag Jevtić1,4, Andria C. Schibler2,4, Gianluca Pegoraro3, Tom Misteli2,*, Daniel L. Levy1,* 1 Department of Molecular Biology, University of Wyoming, Laramie, WY, 82071 2 National Cancer Institute, NIH, Bethesda, MD, 20892 3 High Throughput Imaging Facility (HiTIF), National Cancer Institute, NIH, Bethesda, MD, 20892 4 Co-first authors *Corresponding authors: Daniel L. Levy Tom Misteli University of Wyoming National Cancer Institute, NIH Department of Molecular Biology Center for Cancer Research 1000 E. University Avenue 41 Library Drive, Bldg. 41, B610 Laramie, WY, 82071 Bethesda, MD, 20892 Phone: 307-766-4806 Phone: 240-760-6669 Fax: 307-766-5098 Fax: 301-496-4951 E-mail: [email protected] E-mail: [email protected] Running Head: ELYS is a nuclear size effector Abbreviations: NE, nuclear envelope; NPC, nuclear pore complex; ER, endoplasmic reticulum; Nup, nucleoporin; FG-Nup, phenylalanine-glycine repeat nucleoporin 1 bioRxiv preprint doi: https://doi.org/10.1101/510230; this version posted January 2, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. -
Nature Reviews Molecular Cell Biology
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Sussex Research Online Murray and Carr, Page 1 Smc5/6: a link between DNA-repair and unidirectional replication? Johanne M. Murray and Antony M. Carr* Genome Damage and Stability Centre, University of Sussex, Brighton, Sussex BN1 9RQ, UK. * Corresponding author. [email protected]. Tel +44 (1)1273 678122 Murray and Carr, Page 2 Preface Of the three structural maintenance of chromosome (SMC) complexes, two regulate chromosome dynamics. The third, Smc5/6, functions in homologous recombination and the completion of DNA replication. The literature suggests that Smc5/6 coordinates DNA repair, in part through post-translational modification of uncharacterised target proteins that can dictate their subcellular localization. Smc5/6 functions to establish DNA damage-dependent cohesion. A nucleolar-specific Smc5/6 function has been proposed because Smc5/6 complex yeast mutants display penetrant phenotypes of rDNA instability. rDNA repeats are replicated unidirectionally. Here we propose that unidirectional replication, combined with global Smc5/6 complex functions can explain the apparent rDNA specificity. Introduction SMC complexes regulate high order chromosome structure. Cohesin maintains the link between replicated sister chromosomes that is essential for equal mitotic segregation. Condensin compacts chromatin prior to mitosis. Smc5/6 complex plays a poorly characterised role in DNA repair. The extensive architectural, structural and sequence similarity between the three SMC complexes suggest common modes of action. There is also an intriguing conservation of domain architecture with bacterial Sbc nucleases and the Mre11-Rad50-Nbs1 (MRN) complex (see Ref.1).