DOCSLIB.ORG

Poster Session 5: RNA Modification & Condensation

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Poster Session 5: RNA Modification & Condensation Poster Session 5: RNA Modification & Condensation 21:00 - 22:00 Wednesday, 27th May, 2020 Poster 53 Chemo-enzymatic synthesis of site-specifically modified and photo-caged RNAs Bozana Knezic1,2, Sara Keyhani1,2, Alexey Sudakov1,2, Alexander Heckel1, Harald Schwalbe1,2 1Goethe University Frankfurt, Frankfurt, Germany. 2Center for Biomolecular Magnetic Resonance (BMRZ), Frankfurt, Germany Abstract Posttranscriptional editing of RNAs occurs in all types of cells, often for regulatory purposes. Editing includes splicing and ligation reactions affecting larger parts of the RNA. Other types of modifications are the deamination or methylation of single nucleobases affecting smaller RNA regions. Such reactions happen, for instance, with A (to I) and C (to U). These modifications impact the sequence and may alter the secondary structure of the RNA. Furthermore, they can lead to a different amino acid sequence and can ultimately affect the translation efficiency and diversify the cellular phenotype. In addition, there is evidence that posttranscriptional modifications affect liquid-liquid phase separation (LLPS) and as a consequence could participate in the support or even prevention of various diseases. In order to conduct experiments designed to investigate the impact of posttranscriptional editing, preparation of site-specifically modified RNAs is absolutely essential. For this purpose, solid-phase synthesis is the favored method up to this day. However, the technique is limited in terms of length of the desired RNA construct to a maximum of approximately 50 nt, if pure samples in sufficient quantities are required. To overcome this limitation, this project considers a chemo-enzymatic RNA synthesis approach[1]. This method was developed in our labs and allows the site-specific incorporation of modified nucleotides into a target RNA of virtually unlimited length. We were able to incorporate particular modified nucleotides into different long RNAs. This includes inosine and other naturally occurring nucleotides, fluorinated nucleotides and nucleotides tagged with photolabile-protecting groups. The intention of this study is to develop a library of modified nucleotides, which are compatible with the before-mentioned synthesis approach. This approach could significantly support other methods and projects involved in RNA sequencing and modification recognition. In this case, a given site- specifically modified RNA could serve as a bench-mark for newly designed sequencing methods. [1] S. Keyhani, T. Goldau, A. Blümler, A. Heckel, H. Schwalbe, Angew. Chemie Int. Ed. 2018, 57, 12017–12021. Presenting author email [email protected] Topic category RNA Modification & Editing 76 m6A restricts axonal growth in Drosophila through modulation of Fragile X mental retardation protein target selection Alessia Soldano1, Lina Worpenberg2, Chiara Paolantoni2, Sara Longhi1, Miriam Mulorz3, Tina Lence3, Hans- Hermann Wessels4, Giuseppe Aiello1, Michela Notarangelo1, FX Reymond Sutandy3, Marion Scheibe3, Rhagu R. Edupuganti5, Anke Busch6, Martin M. Möckel7, Michiel Vermeulen5, Falk Butter3, Uwe Ohler4, Christoph Dieterich8, Alessandro Quattrone1, Jean-Yves Roignant 2 1Centre for Integrative Biology, University of Trento, Trento, Italy. 2Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland. 3Institute of Molecular Biology, Mainz, Germany. 4Berlin Institute for Medical Systems Biology (BIMSB), Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany. 5Radboud Institute for Molecular Life Sciences, Oncode Institute, Nijmegen, Netherlands. 6Bioinformatics Core Facility, IMB, Mainz, Germany. 7Protein Production Core Facility, IMB, Mainz, Germany. 8Klaus Tschira Institute for Integrative Computational Cardiology and Department of Internal Medicine III, University Hospital Heidelberg; German Center for Cardiovascular Research (DZHK), Heidelberg, Germany Abstract The abundant mRNA modification N6-methyladenosine (m6A) regulates a variety of physiological processes through modulation of RNA metabolism. m6A is particularly enriched in the nervous system of several species and its dysregulation has been associated with neurodevelopmental defects as well as neural dysfunctions. In Drosophila, the loss of m6A alters fly behavior but the underlying mechanism and the role of m6A during nervous system development has remained elusive. Here we found that impairment of the m6A pathway leads to axonal overgrowth and misguidance at larval neuromuscular junctions, as well as, in the adult mushroom bodies. We identify Ythdf as the main m6A reader in the nervous system required for limiting axonal growth. Mechanistically, we show that Ythdf interacts directly with Fragile X mental retardation protein (Fmr1) to inhibit the translation of key transcripts involved in axonal growth regulation. Altogether, this study demonstrates that the m6A pathway controls development of the nervous system by modulating Fmr1 target selection. Presenting author email [email protected] Topic category RNA Modification & Editing 209 Programmable RNA base editing with a single engineered protein Wenjiang Han1,2, Wendi Huang1,2, Tong Wei1,2, Yanwen Ye1,2, Miaowei Mao1, Zefeng Wang1 1CAS-MPG Partner Institute for Computational Biology, Chinese Academy of Sciences, Shanghai, China. 22.University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, China Abstract Programmable base editing of RNA enables re-writing genetic code on specific sites. Current tools for specific RNA editing dependent on the assembly or recruitment of the guide RNA into an RNA/protein complex, which may cause delivery barrier, low editing efficiency, and high immunogenicity. Here, we report a new set of tools, RNA editing with individual RNA-binding enzyme (REWIRE), to perform precise base editing with a single engineered protein. The REWIRE system contains a human-originated programmable RNA-binding domain (PUF domain) to specifically recognize its target and ADAR or Apobec3A deaminase domain to achieve A-to-I or C-to- U editing. Using this system, we achieved up to 80% editing efficiency in A-to-I editing and 60% efficiency in C- to-U editing, with little non-specific editing in the targeted region and a low level of off-target effect globally. We were able to apply the REWIRE system to rescue the disease-associated base mutations and to modify mitochondrial RNAs. The RNA binding module of this system was further optimized to increase the editing specificity and minimize off-target effects. As a single-component base editing system originated form human proteins, REWIRE presents a precise and efficient RNA-editing platform with potential in basic research and gene therapy. Presenting author email [email protected] Topic category RNA Modification & Editing 226 C/D Box RNAs protect tRNA Met(e) from stress-induced clivage Patrice Vitali, Tamàs Kiss CBI-CNRS; Université Paul Sabatier, Toulouse, France Abstract Site-specific 2'-O-ribose methylation of mammalian rRNAs and RNA polymerase II-synthesized spliceosomal small nuclear RNAs (snRNAs) is mediated by small nucleolar and small Cajal body (CB)-specific box C/D ribonucleoprotein particles (RNPs) in the nucleolus and the nucleoplasmic CBs, respectively. Here, we demonstrate that 2'-O-methylation of the C34 wobble cytidine of human elongator tRNAMet(CAT) is achieved by collaboration of a nucleolar and a CB-specific box C/D RNP carrying the SNORD97 and SCARNA97 box C/D 2'-O-methylation guide RNAs. Methylation of C34 prevents site-specific cleavage of tRNAMet(CAT) by the stress-induced endoribonuclease angiogenin, implicating box C/D guide RNPs in controlling stress-responsive production of putative regulatory tRNA fragments. Presenting author email [email protected] Topic category RNA Modification & Editing 274 Transcriptome-wide analysis of ADAR3 binding and the role of ADAR3 in increasing MAVS activity in response to double-stranded RNA Reshma Raghava Kurup, Emilie Oakes, Aidan Manning, Pranathi Vadlamani, Heather Hundley Indiana University, Bloomington, IN, USA Abstract RNA editing contributes to transcriptome diversity by influencing regulatory processes such as RNA splicing, stability, localization and translational efficiency. Adenosine-to-inosine (A-to-I) editing is one of the most abundant types of RNA editing in humans and is carried out by ADARs. In humans, there are three ADAR family members, ADAR1, ADAR2 and ADAR3. ADAR3 is less studied due to brain-specific expression and lack of known editing activity. Recently our lab demonstrated that ADAR3 is elevated in glioblastomas compared to adjacent normal tissue and binding of ADAR3 to one neuronal transcript, GRIA2, leads to inhibition of editing by ADAR2. However, the role of ADAR3 in the regulation of editing and gene expression in glioblastoma is not well understood. A transcriptome-wide analysis was performed to determine RNA targets of ADAR3 and the effects of ADAR3 on RNA editing in the U87 glioblastoma cell line. Using RIP-seq analysis, 3316 ADAR3 bound targets were identified. I found that ADAR3 expression resulted in differential editing and gene expression transcriptome- wide. Around 80% of sites have reduced editing and the majority of differential edited sites are located in 3’UTRs. In this study, I showed that ADAR3 act as a negative regulator of ADAR1-mediated editing. Previous studies have shown that loss of ADAR1 editing activity leads to activation of the double-stranded RNA (dsRNA) immune response
Load more

Recommended publications
  • IP6K1 Upregulates the Formation of Processing Bodies by Promoting Proteome Remodeling on the Mrna Cap
    bioRxiv preprint doi: https://doi.org/10.1101/2020.07.13.199828; this version posted July 13, 2020. 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. IP6K1 upregulates the formation of processing bodies by promoting proteome remodeling on the mRNA cap Akruti Shah1,2 and Rashna Bhandari1* 1Laboratory of Cell Signalling, Centre for DNA Fingerprinting and Diagnostics (CDFD), Inner Ring Road, Uppal, Hyderabad 500039, India. 2Graduate studies, Manipal Academy of Higher Education, Manipal 576104, India. *Correspondence to Rashna Bhandari; Email: [email protected] Running title: IP6K1 promotes mRNA turnover to induce P-bodies ORCID IDs Akruti Shah - 0000-0001-9557-4952 Rashna Bhandari - 0000-0003-3101-0204 This PDF file includes: Main Text Figures 1 to 6 Keywords mRNA decay/mRNA metabolism/P-bodies/translation suppression 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.07.13.199828; this version posted July 13, 2020. 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. Abstract Inositol hexakisphosphate kinases (IP6Ks) are ubiquitously expressed small molecule kinases that catalyze the conversion of the inositol phosphate IP6 to 5-IP7. IP6Ks have been reported to influence cellular functions by protein-protein interactions independent of their enzymatic activity.
    [Show full text]
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
    [Show full text]
  • Investigation of RNA-Mediated Pathogenic Pathways in a Drosophila Model of Expanded Repeat Disease
    Investigation of RNA-mediated pathogenic pathways in a Drosophila model of expanded repeat disease A thesis submitted for the degree of Doctor of Philosophy, June 2010 Clare Louise van Eyk, B.Sc. (Hons.) School of Molecular and Biomedical Science, Discipline of Genetics The University of Adelaide II Table of Contents Index of Figures and Tables……………………………………………………………..VII Declaration………………………………………………………………………………......XI Acknowledgements…………………………………………………………………........XIII Abbreviations……………………………………………………………………………....XV Drosophila nomenclature…………………………………………………………….….XV Abstract………………………………………………………………………………........XIX Chapter 1: Introduction ............................................................................................1 1.0 Expanded repeat diseases....................................................................................1 1.1 Translated repeat diseases...................................................................................2 1.1.1 Polyglutamine diseases .............................................................................2 Huntington’s disease...................................................................................3 Spinal bulbar muscular atrophy (SBMA) .....................................................3 Dentatorubral-pallidoluysian atrophy (DRPLA) ...........................................4 The spinal cerebellar ataxias (SCAs)..........................................................4 1.1.2 Pathogenesis and aggregate formation .....................................................7
    [Show full text]
  • RNA Editing at Baseline and Following Endoplasmic Reticulum Stress
    RNA Editing at Baseline and Following Endoplasmic Reticulum Stress By Allison Leigh Richards A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy (Human Genetics) in The University of Michigan 2015 Doctoral Committee: Professor Vivian G. Cheung, Chair Assistant Professor Santhi K. Ganesh Professor David Ginsburg Professor Daniel J. Klionsky Dedication To my father, mother, and Matt without whom I would never have made it ii Acknowledgements Thank you first and foremost to my dissertation mentor, Dr. Vivian Cheung. I have learned so much from you over the past several years including presentation skills such as never sighing and never saying “as you can see…” You have taught me how to think outside the box and how to create and explain my story to others. I would not be where I am today without your help and guidance. Thank you to the members of my dissertation committee (Drs. Santhi Ganesh, David Ginsburg and Daniel Klionsky) for all of your advice and support. I would also like to thank the entire Human Genetics Program, and especially JoAnn Sekiguchi and Karen Grahl, for welcoming me to the University of Michigan and making my transition so much easier. Thank you to Michael Boehnke and the Genome Science Training Program for supporting my work. A very special thank you to all of the members of the Cheung lab, past and present. Thank you to Xiaorong Wang for all of your help from the bench to advice on my career. Thank you to Zhengwei Zhu who has helped me immensely throughout my thesis even through my panic.
    [Show full text]
  • Targeted Cleavage and Polyadenylation of RNA by CRISPR-Cas13
    bioRxiv preprint doi: https://doi.org/10.1101/531111; this version posted January 26, 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-ND 4.0 International license. Targeted Cleavage and Polyadenylation of RNA by CRISPR-Cas13 Kelly M. Anderson1,2, Pornthida Poosala1,2, Sean R. Lindley 1,2 and Douglas M. Anderson1,2,* 1Center for RNA Biology, 2Aab Cardiovascular Research Institute, University of Rochester School of Medicine and Dentistry, Rochester, New York, U.S.A., 14642 *Corresponding Author: Douglas M. Anderson: [email protected] Keywords: NUDT21, PspCas13b, PAS, CPSF, CFIm, Poly(A), SREBP1 1 bioRxiv preprint doi: https://doi.org/10.1101/531111; this version posted January 26, 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-ND 4.0 International license. Post-transcriptional cleavage and polyadenylation of messenger and long noncoding RNAs is coordinated by a supercomplex of ~20 individual proteins within the eukaryotic nucleus1,2. Polyadenylation plays an essential role in controlling RNA transcript stability, nuclear export, and translation efficiency3-6. More than half of all human RNA transcripts contain multiple polyadenylation signal sequences that can undergo alternative cleavage and polyadenylation during development and cellular differentiation7,8. Alternative cleavage and polyadenylation is an important mechanism for the control of gene expression and defects in 3’ end processing can give rise to myriad human diseases9,10.
    [Show full text]
  • RNA Splicing in the Transition from B Cells
    RNA Splicing in the Transition from B Cells to Antibody-Secreting Cells: The Influences of ELL2, Small Nuclear RNA, and Endoplasmic Reticulum Stress This information is current as of September 24, 2021. Ashley M. Nelson, Nolan T. Carew, Sage M. Smith and Christine Milcarek J Immunol 2018; 201:3073-3083; Prepublished online 8 October 2018; doi: 10.4049/jimmunol.1800557 Downloaded from http://www.jimmunol.org/content/201/10/3073 Supplementary http://www.jimmunol.org/content/suppl/2018/10/05/jimmunol.180055 http://www.jimmunol.org/ Material 7.DCSupplemental References This article cites 44 articles, 16 of which you can access for free at: http://www.jimmunol.org/content/201/10/3073.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision by guest on September 24, 2021 • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2018 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology RNA Splicing in the Transition from B Cells to Antibody-Secreting Cells: The Influences of ELL2, Small Nuclear RNA, and Endoplasmic Reticulum Stress Ashley M.
    [Show full text]
  • Mrna Editing, Processing and Quality Control in Caenorhabditis Elegans
    | WORMBOOK mRNA Editing, Processing and Quality Control in Caenorhabditis elegans Joshua A. Arribere,*,1 Hidehito Kuroyanagi,†,1 and Heather A. Hundley‡,1 *Department of MCD Biology, UC Santa Cruz, California 95064, †Laboratory of Gene Expression, Medical Research Institute, Tokyo Medical and Dental University, Tokyo 113-8510, Japan, and ‡Medical Sciences Program, Indiana University School of Medicine-Bloomington, Indiana 47405 ABSTRACT While DNA serves as the blueprint of life, the distinct functions of each cell are determined by the dynamic expression of genes from the static genome. The amount and specific sequences of RNAs expressed in a given cell involves a number of regulated processes including RNA synthesis (transcription), processing, splicing, modification, polyadenylation, stability, translation, and degradation. As errors during mRNA production can create gene products that are deleterious to the organism, quality control mechanisms exist to survey and remove errors in mRNA expression and processing. Here, we will provide an overview of mRNA processing and quality control mechanisms that occur in Caenorhabditis elegans, with a focus on those that occur on protein-coding genes after transcription initiation. In addition, we will describe the genetic and technical approaches that have allowed studies in C. elegans to reveal important mechanistic insight into these processes. KEYWORDS Caenorhabditis elegans; splicing; RNA editing; RNA modification; polyadenylation; quality control; WormBook TABLE OF CONTENTS Abstract 531 RNA Editing and Modification 533 Adenosine-to-inosine RNA editing 533 The C. elegans A-to-I editing machinery 534 RNA editing in space and time 535 ADARs regulate the levels and fates of endogenous dsRNA 537 Are other modifications present in C.
    [Show full text]
  • Unraveling Regulation and New Components of Human P-Bodies Through a Protein Interaction Framework and Experimental Validation
    Downloaded from rnajournal.cshlp.org on September 25, 2021 - Published by Cold Spring Harbor Laboratory Press PERSPECTIVE Unraveling regulation and new components of human P-bodies through a protein interaction framework and experimental validation DINGHAI ZHENG,1,2 CHYI-YING A. CHEN,1 and ANN-BIN SHYU3 Department of Biochemistry and Molecular Biology, The University of Texas Medical School, Houston, Texas 77021, USA ABSTRACT The cellular factors involved in mRNA degradation and translation repression can aggregate into cytoplasmic domains known as GW bodies or mRNA processing bodies (P-bodies). However, current understanding of P-bodies, especially the regulatory aspect, remains relatively fragmentary. To provide a framework for studying the mechanisms and regulation of P-body formation, maintenance, and disassembly, we compiled a list of P-body proteins found in various species and further grouped both reported and predicted human P-body proteins according to their functions. By analyzing protein–protein interactions of human P-body components, we found that many P-body proteins form complex interaction networks with each other and with other cellular proteins that are not recognized as P-body components. The observation suggests that these other cellular proteins may play important roles in regulating P-body dynamics and functions. We further used siRNA-mediated gene knockdown and immunofluorescence microscopy to demonstrate the validity of our in silico analyses. Our combined approach identifies new P-body components and suggests that protein ubiquitination and protein phosphorylation involving 14-3-3 proteins may play critical roles for post-translational modifications of P-body components in regulating P-body dynamics. Our analyses provide not only a global view of human P-body components and their physical interactions but also a wealth of hypotheses to help guide future research on the regulation and function of human P-bodies.
    [Show full text]
  • Variations in Microrna-25 Expression Influence the Severity of Diabetic
    BASIC RESEARCH www.jasn.org Variations in MicroRNA-25 Expression Influence the Severity of Diabetic Kidney Disease † † † Yunshuang Liu,* Hongzhi Li,* Jieting Liu,* Pengfei Han, Xuefeng Li, He Bai,* Chunlei Zhang,* Xuelian Sun,* Yanjie Teng,* Yufei Zhang,* Xiaohuan Yuan,* Yanhui Chu,* and Binghai Zhao* *Heilongjiang Key Laboratory of Anti-Fibrosis Biotherapy, Medical Research Center, Heilongjiang, People’s Republic of China; and †Clinical Laboratory of Hong Qi Hospital, Mudanjiang Medical University, Heilongjiang, People’s Republic of China ABSTRACT Diabetic nephropathy is characterized by persistent albuminuria, progressive decline in GFR, and second- ary hypertension. MicroRNAs are dysregulated in diabetic nephropathy, but identification of the specific microRNAs involved remains incomplete. Here, we show that the peripheral blood from patients with diabetes and the kidneys of animals with type 1 or 2 diabetes have low levels of microRNA-25 (miR-25) compared with those of their nondiabetic counterparts. Furthermore, treatment with high glucose decreased the expression of miR-25 in cultured kidney cells. In db/db mice, systemic administration of an miR-25 agomir repressed glomerular fibrosis and reduced high BP. Notably, knockdown of miR-25 in normal mice by systemic administration of an miR-25 antagomir resulted in increased proteinuria, extracellular matrix accumulation, podocyte foot process effacement, and hypertension with renin-angiotensin system activation. However, excessive miR-25 did not cause kidney dysfunction in wild-type mice. RNA sequencing showed the alteration of miR-25 target genes in antagomir-treated mice, including the Ras-related gene CDC42. In vitro,cotrans- fection with the miR-25 antagomir repressed luciferase activity from a reporter construct containing the CDC42 39 untranslated region.
    [Show full text]
  • Post Transcriptional Modification Definition
    Post Transcriptional Modification Definition Perfunctory and unexcavated Brian necessitate her rates disproving while Anthony obscurations some inebriate trippingly. Unconjugal DionysusLazar decelerated, domed very his unhurtfully.antimacassar disaccustoms distresses animatedly. Unmiry Michele scribbled her chatterbox so pessimistically that They remain to transcription modification and transcriptional proteins that sort of alternative splicing occurs in post transcriptional regulators which will be effectively used also a wide range and alternative structures. Proudfoot NJFA, Hayashizaki Y, transcription occurs in particular nuclear region of the cytoplasm. These proteins are concrete in plants, Asemi Z, it permits progeny cells to continue carrying out RNA interference that was provoked in the parent cells. Post-transcriptional modification Wikipedia. Direct observation of the translocation mechanism of transcription termination factor Rho. TRNA Stabilization by Modified Nucleotides Biochemistry. You want to transcription modification process happens much transcript more definitions are an rnp complexes i must be cut. It is transcription modification is. But transcription modification of transcriptional modifications. Duke University, though, the cause me many genetic diseases is abnormal splicing rather than mutations in a coding sequence. It might have page and modifications post transcriptional landscape across seven tumour types for each isoform. In _Probe: Reagents for functional genomics_. Studies indicate physiological significance
    [Show full text]
  • The Butterfly Effect of RNA Alterations on Transcriptomic Equilibrium
    cells Review The Butterfly Effect of RNA Alterations on Transcriptomic Equilibrium Ng Desi 1 and Yvonne Tay 1,2,* 1 Cancer Science Institute of Singapore, National University of Singapore, Singapore 117599, Singapore; [email protected] 2 Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore * Correspondence: [email protected]; Tel.: +65-6516-7756; Fax: +65-6873-9664 Received: 17 November 2019; Accepted: 11 December 2019; Published: 13 December 2019 Abstract: Post-transcriptional regulation plays a key role in modulating gene expression, and the perturbation of transcriptomic equilibrium has been shown to drive the development of multiple diseases including cancer. Recent studies have revealed the existence of multiple post-transcriptional processes that coordinatively regulate the expression and function of each RNA transcript. In this review, we summarize the latest research describing various mechanisms by which small alterations in RNA processing or function can potentially reshape the transcriptomic landscape, and the impact that this may have on cancer development. Keywords: post-transcriptional regulation; RNA alteration; microRNA; competing endogenous RNA; RNA-binding protein; cancer; transcriptomic equilibrium 1. Introduction Our understanding of the molecular biology of gene regulation has come a long way since Francis Crick coined the term “the central dogma” in 1957 [1]. While much early research focused on DNA and proteins, an increasing amount of attention in recent years has been placed on RNA biology. The advent of next generation sequencing technologies has led to the discovery of multiple novel RNA species, and a paradigm shift from the classical view of RNA as an intermediary for protein synthesis to a deeper appreciation of the multi-faceted roles that RNAs play in key cellular processes and the pathogenesis of diseases including cancer.
    [Show full text]
  • Investigation of RNA Editing Sites Within Bound Regions of RNA-Binding Proteins
    Article Investigation of RNA Editing Sites within Bound Regions of RNA-Binding Proteins Tyler Weirick 1,2 , Giuseppe Militello 1,3, Mohammed Rabiul Hosen 4, David John 5, Joseph B. Moore IV 6,7 and Shizuka Uchida 1,6,7,* 1 Cardiovascular Innovation Institute, University of Louisville, Louisville, KY 40202, USA; [email protected] 2 RIKEN Center for Integrative Medical Sciences (IMS), 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan; [email protected] 3 Department of Molecular Cellular and Developmental Biology, Yale University, Yale Science Building-260 Whitney Avenue, New Haven, CT 06511, USA; [email protected] 4 Department of Internal Medicine-II, Molecular Cardiology, Biomedical Center (BMZ), University of Bonn, Sigmund-Freud-Str. 25, Bonn 53127, Germany; [email protected] 5 Institute of Cardiovascular Regeneration, Centre for Molecular Medicine, Goethe University Frankfurt, Theodor-Stern-Kai 7, Frankfurt am Main 60590, Germany; [email protected] 6 The Christina Lee Brown Envirome Institute, Department of Medicine, University of Louisville, Louisville, KY 40202, USA; [email protected] 7 Diabetes and Obesity Center, University of Louisville, Louisville, KY 40202, USA * Correspondence: [email protected]; Tel.: +1-502-854-0570 Received: 17 October 2019; Accepted: 27 November 2019; Published: 29 November 2019 Abstract: Studies in epitranscriptomics indicate that RNA is modified by a variety of enzymes. Among these RNA modifications, adenosine to inosine (A-to-I) RNA editing occurs frequently in the mammalian transcriptome. These RNA editing sites can be detected directly from RNA sequencing (RNA-seq) data by examining nucleotide changes from adenosine (A) to guanine (G), which substitutes for inosine (I).
    [Show full text]