Annotating RNA Motifs in Sequences and Alignments Paul P

Total Page:16

File Type:pdf, Size:1020Kb

Annotating RNA Motifs in Sequences and Alignments Paul P Published online Xxxx 2014 Nucleic Acids Research, 2014, Vol. XX, No. YY 1–37 doi:10.1093/nar/gkn000 Supplementary material: Annotating RNA motifs in sequences and alignments Paul P. Gardner1;∗, and Hisham Eldai1∗ 1School of Biological Sciences, Biomolecular Interaction Centre, University of Canterbury, Private Bag 4800, Christchurch 8140, New Zealand Received July, 2014; Revised July, 2014; Accepted July, 2014 ∗To whom correspondence should be addressed. Tel: +64 3 364 2987; Fax: +64 3 364 2590; Email: [email protected] c 2014 The Author(s) This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/ by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. [11:22 5/11/2014 supplementary-results.tex] Page: 1 1{37 2 Nucleic Acids Research, 2014, Vol. XX, No. YY SUMMARY In the following document we present supplementary methods, results and figures relating to the RMfam resource: 1. Figures 1-8 illustrate secondary structure diagrams for each of the RMfam motifs. Figure 1 contains a Legend, detailing the color and symbol schemes used to illustrate different evolutionary constraints on the different structures. 2. Figure 9 illustrates our estimates of the accuracy of using covariance models to annotate RNA motifs on sequences and alignments. 3. Figures 10-43 contain secondary structures and the results of per-motif benchmarks. 4. Figures 44&45 illustrate improvements to Rfam (v11.0) alignments and consensus structures based upon RMfam annotations. 5. Figure 46 illustrates the network of the 50 highest scoring RMfam to Rfam mappings. [11:22 5/11/2014 supplementary-results.tex] Page: 2 1{37 Nucleic Acids Research, 2014, Vol. XX, No. YY 3 SECONDARY STRUCTURES Legend U U U Y C G A A A U C basepairannotations A A G A U G C G U C covaryingmutations G C Y R C G compatiblemutations G Y C G nomutationsobserved A Y R Y G C nucleotide nucleotide U A A R present identity A U Y 80% 60% N 80% 70% 40% N 70% R U G U N 60% 5´ 5´ 5´ 5´ 5´ R=AorG.Y=CorU. Figure 1. A legend describing the symbols used in all the secondary structures images presented in figures 1-8. Secondary structure diagrams of: tetraloops: ANYA (1, 2, 3), CUYG (4, 5, 6, 7), GNRA (8, 9, 10, 11, 12, 13), UMAC (14, 15) and UNCG (10, 12, 13, 16) and the hairpins loops C-loop (17, 18, 19, 20), T-loop (12, 13, 21, 22, 23) and U-turn (12, 13, 24, 25). 5-46 nt R R R A U R U R Y R G A G C C G C U A G C A R R Y R Y C A U R G Y 5´ 5´ 5´ Figure 2. Secondary structure diagrams of: the hairpins loops; C-loop (17, 18, 19, 20), T-loop (12, 13, 21, 22, 23) and U-turn (12, 13, 24, 25). 0-38 nt Y 3-81 nt R C R C 4-40 nt R R Y A A Y G C A U G R Y G G C Y R Y R U U R Y Y C C A G G C R R Y G A A A Y R R Y G U A A A G U A U G G G G R A A G G 0-57 nt G A G A A Y R R R Y C G R R R R Y R R Y Y R R Y R R Y C G Y R A R R Y C G G C A G 5´ 5´ 5´ A G 5´ R A R A A 5´ R Figure 3. Secondary structure diagrams of: internal loops: three k-turns (3, 12, 13, 18, 26, 27, 28) and two sarcin-ricin loops (12, 20, 29, 30). [11:22 5/11/2014 supplementary-results.tex] Page: 3 1{37 4 Nucleic Acids Research, 2014, Vol. XX, No. YY R Y G G A G G G G C 4-88 nt 2-22 nt R G Y Y G A G A U C A G A A G U C C C G G G A C U C G G R Y R Y A G R R C G R G R Y A A R Y R R A 0-31 nt C A A C G R Y R Y R G G Y U G U G C C C C A A A U R Y A R Y G G U G A A 28-249 nt R G A A R Y A G C G G A G 1-12 nt A R Y C Y C G G Y Y A G C R Y C R 0-7 nt G Y A G A Y U R R Y Y G R Y G A G C Y G C G Y G U G 0-36 nt C G Y G U G R Y G Y G C G Y G C R G C 5´ R Y A 5´ G C 5´ R G C Y R 5´ 5´ 5´ Figure 4. Secondary structure diagrams of: internal loops: the tandem-GA (20, 31), twist up (17) and UAA GAN (32), the docking elbow (33), right angle 2 and 3 (34) motifs. R Y R R R Y C G C G C G R Y Y R C G Y R A U A U R Y R Y Y G A U C G C G G C C G G Y A U A U G C A U A U R Y C G G C A U R Y A U A U A U G C R U C G A U G C 5´ U Y U Y R U 5´ U U U Y 5´ R Y Y Y Y R R R R Figure 5. Secondary structure diagrams of Rho independent transcription terminators (35). [11:22 5/11/2014 supplementary-results.tex] Page: 4 1{37 Nucleic Acids Research, 2014, Vol. XX, No. YY 5 A R A R G Y G Y R G A U U A U U C G Y A Y R U R U Y Y G U A U A U Y U A R U R U RA Y R Y R R Y U A R U R R Y U R U R U R 5´ 5´ U 5´ 5´ U R G C G Y R 5´ 5´ A A Y A A R A A C A A A R R Figure 6. Secondary structure diagrams of: interactions: the AUF1 (36), CRC (37, 38, 39), CsrA (40, 41, 42, 43, 44, 45, 46, 47), HuR (48, 49), Roquin (50) and VTS1 (51, 52, 53, 54) protein binding motifs. R A A A G A R G A Y R G A G G C C G A C R Y A C A U Y Y G R Y C G R G Y R R Y Y C C C Y C G A A Y G R G A R C R C G R Y G U R Y A U G Y Y G Y 5´ A U A U G Y C 5´ 5´ Figure 7. Secondary structure diagrams of: vapC target (55), the SRP RNA S domain (56, 57, 58) and the catalytic Domain-V (59, 60). [11:22 5/11/2014 supplementary-results.tex] Page: 5 1{37 6 Nucleic Acids Research, 2014, Vol. XX, No. YY Shine-Dalgarno sequence from Bacillus subtilis subsp. subtilis str. 168 2.0 1.0 bits AA GG G A A A A G U A A G A U U A A U A A U U AAAU C A AU U U GA U A C U U CA U U AUAAAAAUAU UU C GA U C C A C G G C C C C C C C C C U C C C U A A G C C CU G UG U GC G UU G G G GGG G C CA G U C G G G A U U A G A G G C 0.0 A -30 -25 -20 -15 -10 -5 0 5 Distance from start codon (nucs) WebLogo 3.1 5´ R A A A R G G G G G R R Y Y R Y A U G A R R R A R Shine-Dalgarno sequence from Escherichia coli str. K-12 substr. MG1655 2.0 1.0 bits AGGA A A A A A A U AA A AA A A U U UU U AA C U UUU G A A AU A U C C C G C UC A U A CC A U U U CA U G U U U G C C G C GU C AA C C A C C G C GC C U UG C U G U G G C CCG UG C U AG CA A U G 0.0 GA -30 -25 -20 -15 -10 -5 0 5 Distance from start codon (nucs) WebLogo 3.1 5´ Y Y Y Y Y Y Y Y R R R G G R R R A Y Y A U G A R A R Shine-Dalgarno sequence from Helicobacter pylori 26695 2.0 1.0 bits A AG A A A AU UA G U A A A UU U AA AU AA U A A C CA A A A U A A U AAAA GG UA AC GU U AUU U U UA UU U G G A AU C CC GC G U G C C G U G U GC C A C G C UC U C C C C U UG U U G G G C G C G C C C G C GG C G C G U C A G G U 0.0 GAA -30 -25 -20 -15 -10 -5 0 5 Distance from start codon (nucs) WebLogo 3.1 5´ Y Y Y Y A A G G R R Y A U G R R A R A Figure 8.
Recommended publications
  • Hunting RNA Motifs
    Hunting RNA motifs Paul Gardner July 23, 2012 Paul Gardner Hunting RNA motifs Classification problems I What is this? I The second most abundant M. tuberculosis transcript I No hits to Rfam, no homologs have been identified, no known function Mycobacteria tuberculosis genome: RNA−seq and annotations 7e+05 +ve strand R ank R eads Gene −ve strand 6e+05 1 5,741K SSU rR N A 2 689K sRNA/RUF? 5e+05 3 236K R N aseP R N A 4e+05 4 197K LSU rR N A 5 119K AT P synthase 3e+05 Read counts 6 119K HSP X 2e+05 7 115K tmR N A CDSs ncRNAs 8 103K Secreted protein 1e+05 Pfam domain terminators 0e+00 Arnvig et al. Rv3661 miscrna00343 (2011) PLoS HAD Rv3662c Pathog. 4099500 4100000 4100500 4101000 4101500 4102000 genome coordinate Paul Gardner Hunting RNA motifs Classification problems I What about this? I The seventh most abundant N. gonorrhoeae transcript I No hits to Rfam, no homologs have been identified, no known function Neisseria gonorrhoeae genome: RNA−seq and annotations R ank R eads Gene 80000 +ve strand −ve strand 1 206K R N aseP R N A 2 178K tR N A -Ser 60000 3 130K ZapA 3‘ U T R ? 4 120K P hage protein 40000 5‘ U T R ? 5 97K tmR N A Read counts 6 93K BRO protein 20000 CDSs ncRNAs 7 81K sR N A ? Pfam domain terminators 8 81K Hsp70 protein 0 9 76K tRNA-Asp NGO2161 terminator12061 terminator12063 Inositol_P terminator12062 NGO2162 terminator12064 Isabella & Clark SEC−C (2011) BMC Genomics.
    [Show full text]
  • Clusters of Bacterial RNA Polymerase Are Biomolecular Condensates That Assemble Through Liquid–Liquid Phase Separation
    Clusters of bacterial RNA polymerase are biomolecular condensates that assemble through liquid–liquid phase separation Anne-Marie Ladouceura,1, Baljyot Singh Parmarb,1, Stefan Biedzinskia, James Walla, S. Graydon Topea, David Cohna, Albright Kima, Nicolas Soubrya, Rodrigo Reyes-Lamothea, and Stephanie C. Webera,b,2 aDepartment of Biology, McGill University, Montreal, QC H3A 1B1, Canada; and bDepartment of Physics, McGill University, Montreal, QC H3A 2T8, Canada Edited by Richard A. Young, Massachusetts Institute of Technology, Cambridge, MA, and approved June 23, 2020 (received for review March 17, 2020) Once described as mere “bags of enzymes,” bacterial cells are in possibility that prokaryotes also use LLPS to compartmentalize fact highly organized, with many macromolecules exhibiting non- their cells. uniform localization patterns. Yet the physical and biochemical In eukaryotes, LLPS is mediated by proteins containing mul- mechanisms that govern this spatial heterogeneity remain largely tivalent domains and disordered regions (22–24) that bring unknown. Here, we identify liquid–liquid phase separation (LLPS) as molecules together into dynamic condensates through transient a mechanism for organizing clusters of RNA polymerase (RNAP) in interactions. Sequence analysis predicts that bacterial proteomes Escherichia coli . Using fluorescence imaging, we show that RNAP have a much lower frequency of disordered regions than quickly transitions from a dispersed to clustered localization pattern eukaryotic proteomes: Only 4.2% compared to 33%, respectively as cells enter log phase in nutrient-rich media. RNAP clusters are (25). This paucity of disorder raises doubts about the prevalence sensitive to hexanediol, a chemical that dissolves liquid-like com- of LLPS in this domain of life.
    [Show full text]
  • Specific and Global RNA Regulators in Pseudomonas Aeruginosa
    International Journal of Molecular Sciences Review Specific and Global RNA Regulators in Pseudomonas aeruginosa Petra Pusic , Elisabeth Sonnleitner and Udo Bläsi * Max Perutz Labs, Department of Microbiology, Immunobiology and Genetics, Centre of Molecular Biology, Vienna Biocenter (VBC), University of Vienna, Dr. Bohrgasse 9/4, 1030 Vienna, Austria; [email protected] (P.P.); [email protected] (E.S.) * Correspondence: [email protected] Abstract: Pseudomonas aeruginosa (Pae) is an opportunistic pathogen showing a high intrinsic resis- tance to a wide variety of antibiotics. It causes nosocomial infections that are particularly detrimental to immunocompromised individuals and to patients suffering from cystic fibrosis. We provide a snapshot on regulatory RNAs of Pae that impact on metabolism, pathogenicity and antibiotic suscep- tibility. Different experimental approaches such as in silico predictions, co-purification with the RNA chaperone Hfq as well as high-throughput RNA sequencing identified several hundreds of regulatory RNA candidates in Pae. Notwithstanding, using in vitro and in vivo assays, the function of only a few has been revealed. Here, we focus on well-characterized small base-pairing RNAs, regulating specific target genes as well as on larger protein-binding RNAs that sequester and thereby modulate the activity of translational repressors. As the latter impact large gene networks governing metabolism, acute or chronic infections, these protein-binding RNAs in conjunction with their cognate proteins are regarded as global post-transcriptional regulators. Keywords: Pseudomonas aeruginosa; base-pairing sRNAs; protein-binding RNAs; Hfq; Crc; RsmA; RsmN/F; post-transcriptional regulation Citation: Pusic, P.; Sonnleitner, E.; Bläsi, U. Specific and Global RNA Regulators in Pseudomonas aeruginosa.
    [Show full text]
  • Characteristics of Genome Evolution in Obligate Insect Symbionts, Including The
    Characteristics of genome evolution in obligate insect symbionts, including the description of a recently identified obligate extracellular symbiont. Thesis Presented in Partial Fulfillment of the Requirements for the Degree Master of Science in the Graduate School of The Ohio State University By Laura Jean Kenyon, B.S. Graduate Program in Evolution, Ecology, and Organismal Biology The Ohio State University 2015 Thesis Committee: Norman Johnson Andy Michel Kelly Wrighton Zakee L. Sabree, Advisor Copyright by Laura Jean Kenyon 2015 Abstract Animal-bacterial symbioses have shaped the evolution of all eukaryotic organisms. All symbioses have in common a long-term association and therefore provide valuable insight into the evolution and diversification of both partners. Insect-bacterial mutualisms represent the most extreme natural partnerships known, showing evidence of coevolution and obligate interdependence between the partners. Early investigations of plant sap-feeding insects, in particular, revealed tissues of unknown function inhabited by bacteria and insects void of their symbionts revealed reduced host fitness compared to symbiotic insects. Due to the obligate nature of the relationships, endosymbiotic bacteria are uncultivable, but complete genome sequencing suggests bacterial mutualists metabolic capabilities and likely contribution to the mutualisms, typically nutrient provisioning. A well-supported pattern of bacterial genome evolution for obligate mutualists is extreme genome reduction, likely due to relaxed selection upon genes that are not required in the stable environment of the host, leading to an accumulation of deleterious mutations in these genes, and eventually to their complete loss, leaving only those genes that are required for the relatively-stable life-style and for maintenance of the symbiosis.
    [Show full text]
  • Structure-Based Mechanisms of Processive Transcription Anti-Termination
    Structure-based mechanisms of processive transcription anti-termination A Dissertation Submitted in Partial Fulfilment of the Requirements for the Degree of Doctor rerum naturalium to the Department of Biology, Chemistry, Pharmacy of Freie Universität Berlin by Yong-Heng Huang Berlin, 2020 Supervisor: Prof. Markus C. Wahl, Ph.D. Second examiner: Prof. Sutapa Chakrabarti, Ph.D. Date of defense: 28.01.2020 Table of Contents 1. Summary .................................................................................................................... 1 Zusammenfassung ......................................................................................................... 3 2. Introduction ................................................................................................................ 5 2.1. RNA polymerase and transcription ................................................................... 5 2.2. Elongation regulations ...................................................................................... 8 2.2.1. Pausing .................................................................................................. 9 2.2.2. Anti-termination .................................................................................... 11 2.3. Nus factors ..................................................................................................... 12 2.4. Life cycle of phage λ and λN-mediated anti-termination .................................. 15 2.5. Ribosomal RNA (rRNA) biogenesis ...............................................................
    [Show full text]
  • Evidence for a Second Class of S-Adenosylmethionine Riboswitches
    Open Access Research2005CorbinoetVolume al. 6, Issue 8, Article R70 Evidence for a second class of S-adenosylmethionine riboswitches comment and other regulatory RNA motifs in alpha-proteobacteria Keith A Corbino*, Jeffrey E Barrick†, Jinsoo Lim*, Rüdiger Welz*‡, Brian J Tucker†, Izabela Puskarz*, Maumita Mandal*§, Noam D Rudnick* and Ronald R Breaker* * Addresses: Department of Molecular, Cellular and Developmental Biology, Yale University, P.O. Box 208103, New Haven, CT 06520-8103, reviews USA. †Department of Molecular Biophysics and Biochemistry, Yale University, P.O. Box 208103, New Haven, CT 06520-8103, USA. ‡Department of Chemistry, Yale University, P.O. Box 208103, New Haven, CT 06520-8103, USA. §Department of Physics, University of California, Berkeley, CA 94720-7200, USA. Correspondence: Ronald R Breaker. E-mail: [email protected] Published: 1 August 2005 Received: 28 April 2005 Revised: 15 June 2005 Genome Biology 2005, 6:R70 (doi:10.1186/gb-2005-6-8-r70) reports Accepted: 1 July 2005 The electronic version of this article is the complete one and can be found online at http://genomebiology.com/2005/6/8/R70 © 2005 Corbino et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. SAM-II<p>Comparativetumefaciensthat is not riboswitches found </it>and insequence Gram-positive and other other analysis α-proteobacteria. RNA bacteria.</p> and motifs structural in bacteriaOne probingof these identifiedRNA elements five RNA is probably elements a SAM-II, in the intergenic the only riboswitch region of <it>Agrobacter class identifiedium so far deposited research Abstract Background: Riboswitches are RNA elements in the 5' untranslated leaders of bacterial mRNAs that directly sense the levels of specific metabolites with a structurally conserved aptamer domain to regulate expression of downstream genes.
    [Show full text]
  • The Biology of RNA-Protein Complexes
    The Biology of RNA-Protein Complexes PROGRAM AND ABSTRACTS October11thͲ14th2017,ThonͲDittmerPalais,Regensburg,Germany GENERAL INFORMATION Throughout this program, the numbers next to the titles refer to corresponding oral or poster abstract numbers in the abstract section of this book. Please refrain from citing the abstracts in bibliographies. The information contained in this abstract book should be treated as personal communicationandshouldbecitedonlywiththeexpressedconsentoftheauthor. Nounauthorizedphotographyinsessions: To encourage the sharing of novel and unpublished data, taking photographs and/or videos during the scientific sessions (both oral andposters),orofpostersoutsidesessionhours,isstrictlyprohibited. Violatorsofthispolicymayhavetheirequipmentconfiscatedand/or theymaybeaskedtoleavetheconferenceandhavetheirregistration privilegesrevokedwithoutreimbursement Useofsocialmedia: Thehashtagis#SFB960.Weencourageallattendeestotweetabout the amazing science they experience at the SFB960 meeting in Regensburg.But,pleasedorespectthefollowingruleswhentweeting orusingothersocialmedia: 1. bepoliteandrespectfulofothersinallofyourmessages 2. donottransmitphotographsofslidesorpostersunderany circumstances 3. donottransmitphotographsofconferenceattendeeswithout theirexpressedconsent 4. tweetersshouldrespectrequestsofpresenterswhoasktorefrain fromtweetingthecontentoftheirtalksorposters CoverPicture:TobiasBeck Ͳ Layout:JanMedenbach Ͳ Print: Offset Haas 2 MEETING SPONSORS 3 SCIENTIFIC ORGANIZERS Prof. Dr.
    [Show full text]
  • New Insights Into Marine Group III Euryarchaeota, from Dark to Light
    The ISME Journal (2017), 1–16 © 2017 International Society for Microbial Ecology All rights reserved 1751-7362/17 www.nature.com/ismej ORIGINAL ARTICLE New insights into marine group III Euryarchaeota, from dark to light Jose M Haro-Moreno1,3, Francisco Rodriguez-Valera1, Purificación López-García2, David Moreira2 and Ana-Belen Martin-Cuadrado1,3 1Evolutionary Genomics Group, Departamento de Producción Vegetal y Microbiología, Universidad Miguel Hernández, Alicante, Spain and 2Unité d’Ecologie, Systématique et Evolution, UMR CNRS 8079, Université Paris-Sud, Orsay Cedex, France Marine Euryarchaeota remain among the least understood major components of marine microbial communities. Marine group II Euryarchaeota (MG-II) are more abundant in surface waters (4–20% of the total prokaryotic community), whereas marine group III Euryarchaeota (MG-III) are generally considered low-abundance members of deep mesopelagic and bathypelagic communities. Using genome assembly from direct metagenome reads and metagenomic fosmid clones, we have identified six novel MG-III genome sequence bins from the photic zone (Epi1–6) and two novel bins from deep-sea samples (Bathy1–2). Genome completeness in those genome bins varies from 44% to 85%. Photic-zone MG-III bins corresponded to novel groups with no similarity, and significantly lower GC content, when compared with previously described deep-MG-III genome bins. As found in many other epipelagic microorganisms, photic-zone MG-III bins contained numerous photolyase and rhodopsin genes, as well as genes for peptide and lipid uptake and degradation, suggesting a photoheterotrophic lifestyle. Phylogenetic analysis of these photolyases and rhodopsins as well as their genomic context suggests that these genes are of bacterial origin, supporting the hypothesis of an MG-III ancestor that lived in the dark ocean.
    [Show full text]
  • Structural and Functional Studies of a Noncanonical Dicer From
    www.nature.com/scientificreports OPEN Structural and functional studies of a noncanonical Dicer from Entamoeba histolytica Received: 20 December 2016 Xiang Yu1,2, Xuhang Li2, Lina Zheng2, Jinbiao Ma2 & Jianhua Gan1 Accepted: 13 February 2017 RNaseIII proteins are dsRNA-specific endonucleases involved in many important biological processes, Published: 20 March 2017 such as small RNA processing and maturation in eukaryotes. Various small RNAs have been identified in a protozoan parasite Entamoeba histolytica. EhRNaseIII is the only RNaseIII endonuclease domain (RIIID)-containing protein in E. histolytica. Here, we present three crystal structures that reveal several unique structural features of EhRNaseIII, especially the interactions between the two helixes (α1 and α7) flanking the RIIID core domain. Structure and sequence analysis indicate thatEh RNaseIII is a noncanonical Dicer and it lacks a dsRBD in the C-terminal region (CTR). In vitro studies suggest that EhRNaseIII prefers to bind and cleave longer dsRNAs, generating products around 25 nucleotides in length. Truncation of the CTR or attaching the dsRBD of Aquifex aeolicus RNaseIII can enhance the binding and cleavage activities of EhRNaseIII. In combination with in vitro crosslinking assay, our results suggested that EhRNaseIII functions in a cooperative mode. We speculate that some partner proteins may exist in E. histolytica and regulates the activity of EhRNaseIII through interaction with its CTR. Our studies support that EhRNaseIII plays an important role in producing small RNAs in E. histolytica. Ribonuclease III (RNaseIII) proteins are metal-ion-dependent, double-stranded (ds) RNA-specific endonucleases1 that are highly conserved in bacteria and eukaryotes. In higher eukaryotes, RNaseIII proteins, such as Dicer and Drosha, play important roles in the RNA interference (RNAi) pathway2.
    [Show full text]
  • Riboregulation in Nitrogen-Fixing Endosymbiotic Bacteria
    microorganisms Review Riboregulation in Nitrogen-Fixing Endosymbiotic Bacteria Marta Robledo 1 , Natalia I. García-Tomsig 2 and José I. Jiménez-Zurdo 2,* 1 Intergenomics Group, Departamento de Biología Molecular, Instituto de Biomedicina y Biotecnología de Cantabria, CSIC-Universidad de Cantabria-Sodercan, 39011 Santander, Spain; [email protected] 2 Structure, Dynamics and Function of Rhizobacterial Genomes (Grupo de Ecología Genética de la Rizosfera), Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas (CSIC), 18008 Granada, Spain; [email protected] * Correspondence: [email protected]; Tel.: +34-958-181-600 Received: 22 January 2020; Accepted: 5 March 2020; Published: 10 March 2020 Abstract: Small non-coding RNAs (sRNAs) are ubiquitous components of bacterial adaptive regulatory networks underlying stress responses and chronic intracellular infection of eukaryotic hosts. Thus, sRNA-mediated regulation of gene expression is expected to play a major role in the establishment of mutualistic root nodule endosymbiosis between nitrogen-fixing rhizobia and legume plants. However, knowledge about this level of genetic regulation in this group of plant-interacting bacteria is still rather scarce. Here, we review insights into the rhizobial non-coding transcriptome and sRNA-mediated post-transcriptional regulation of symbiotic relevant traits such as nutrient uptake, cell cycle, quorum sensing, or nodule development. We provide details about the transcriptional control and protein-assisted activity mechanisms of the functionally characterized sRNAs involved in these processes. Finally, we discuss the forthcoming research on riboregulation in legume symbionts. Keywords: rhizobia; Sinorhizobium (Ensifer) meliloti; α-proteobacteria; legumes; sRNA; non-coding RNA; dRNA-Seq; RNA-binding proteins; RNases 1. Introduction Some soil-dwelling species of the large classes of α- and β-proteobacteria, collectively referred to as rhizobia, establish mutualistic symbioses with legumes.
    [Show full text]
  • Identification of Chromosomal Alpha-Proteobacterial Small Rnas by Comparative Genome Analysis and Detection in Sinorhizobium Meliloti Strain 1021
    Identification of chromosomal alpha-proteobacterial small RNAs by comparative genome analysis and detection in Sinorhizobium meliloti strain 1021. Vincent Ulvé, Emeric Sevin, Angélique Chéron, Frédérique Barloy-Hubler To cite this version: Vincent Ulvé, Emeric Sevin, Angélique Chéron, Frédérique Barloy-Hubler. Identification of chromoso- mal alpha-proteobacterial small RNAs by comparative genome analysis and detection in Sinorhizobium meliloti strain 1021.. BMC Genomics, BioMed Central, 2007, 8, pp.467. 10.1186/1471-2164-8-467. hal-00257380 HAL Id: hal-00257380 https://hal.archives-ouvertes.fr/hal-00257380 Submitted on 26 Nov 2010 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. BMC Genomics BioMed Central Research article Open Access Identification of chromosomal alpha-proteobacterial small RNAs by comparative genome analysis and detection in Sinorhizobium meliloti strain 1021 Vincent M Ulvé†1, Emeric W Sevin†1, Angélique Chéron1 and Frédérique Barloy-Hubler*1,2 Address: 1CNRS UMR6061 Génétique et Développement, Groupe Modèles Génétiques, Université
    [Show full text]
  • Transcription Termination and Antitermination of Bacterial CRISPR
    RESEARCH ARTICLE Transcription termination and antitermination of bacterial CRISPR arrays Anne M Stringer1, Gabriele Baniulyte2, Erica Lasek-Nesselquist1, Kimberley D Seed3,4, Joseph T Wade1,2* 1Wadsworth Center, New York State Department of Health, Albany, United States; 2Department of Biomedical Sciences, School of Public Health, University at Albany, Albany, United States; 3Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, United States; 4Chan Zuckerberg Biohub, San Francisco, United States Abstract A hallmark of CRISPR-Cas immunity systems is the CRISPR array, a genomic locus consisting of short, repeated sequences (‘repeats’) interspersed with short, variable sequences (‘spacers’). CRISPR arrays are transcribed and processed into individual CRISPR RNAs that each include a single spacer, and direct Cas proteins to complementary sequences in invading nucleic acid. Most bacterial CRISPR array transcripts are unusually long for untranslated RNA, suggesting the existence of mechanisms to prevent premature transcription termination by Rho, a conserved bacterial transcription termination factor that rapidly terminates untranslated RNA. We show that Rho can prematurely terminate transcription of bacterial CRISPR arrays, and we identify a widespread antitermination mechanism that antagonizes Rho to facilitate complete transcription of CRISPR arrays. Thus, our data highlight the importance of transcription termination and antitermination in the evolution of bacterial CRISPR-Cas systems. *For correspondence: Introduction [email protected] CRISPR-Cas systems are adaptive immune systems found in many bacteria and archaea (Wright et al., 2016). The hallmark of CRISPR-Cas systems is the CRISPR array, which is composed Competing interests: The of multiple alternating, short, identical ‘repeat’ sequences, interspersed with short, variable ‘spacer’ authors declare that no sequences.
    [Show full text]