5
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Ancient Transcription Factors in the News

      review-article
      a , , b
      mBio
      American Society for Microbiology
      NusG, RfaH, antitermination, transcription, translation

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          In every cell from bacteria to mammals, NusG-like proteins bind transcribing RNA polymerase to modulate the rate of nascent RNA synthesis and to coordinate it with numerous cotranscriptional processes that ultimately determine the transcript fate. Housekeeping NusG factors regulate expression of the bulk of the genome, whereas their highly specialized paralogs control just a few targets.

          ABSTRACT

          In every cell from bacteria to mammals, NusG-like proteins bind transcribing RNA polymerase to modulate the rate of nascent RNA synthesis and to coordinate it with numerous cotranscriptional processes that ultimately determine the transcript fate. Housekeeping NusG factors regulate expression of the bulk of the genome, whereas their highly specialized paralogs control just a few targets. In Escherichia coli, NusG stimulates silencing of horizontally acquired genes, while its paralog RfaH counters NusG action by activating a subset of these genes. Acting alone or as part of regulatory complexes, NusG factors can promote uninterrupted RNA synthesis, bring about transcription pausing or premature termination, modulate RNA processing, and facilitate translation. Recent structural and mechanistic studies of NusG homologs from all domains of life reveal molecular details of multifaceted interactions that underpin their unexpectedly diverse regulatory roles. NusG proteins share conserved binding sites on RNA polymerase and many effects on the transcription elongation complex but differ in their mechanisms of recruitment, interactions with nucleic acids and secondary partners, and regulatory outcomes. Strikingly, some can alternate between autoinhibited and activated states that possess dramatically different secondary structures to achieve exquisite target specificity.

          Related collections

          Most cited references123

          • Record: found
          • Abstract: found
          • Article: not found

          Bacterial sigma factors: a historical, structural, and genomic perspective.

          Transcription initiation is the crucial focal point of gene expression in prokaryotes. The key players in this process, sigma factors (σs), associate with the catalytic core RNA polymerase to guide it through the essential steps of initiation: promoter recognition and opening, and synthesis of the first few nucleotides of the transcript. Here we recount the key advances in σ biology, from their discovery 45 years ago to the most recent progress in understanding their structure and function at the atomic level. Recent data provide important structural insights into the mechanisms whereby σs initiate promoter opening. We discuss both the housekeeping σs, which govern transcription of the majority of cellular genes, and the alternative σs, which direct RNA polymerase to specialized operons in response to environmental and physiological cues. The review concludes with a genome-scale view of the extracytoplasmic function σs, the most abundant group of alternative σs.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Structure of paused transcription complex Pol II-DSIF-NELF

            Metazoan gene regulation often involves pausing of RNA polymerase II (Pol II) in the promoter-proximal region. Paused Pol II is stabilized by the protein complexes DRB sensitivity-inducing factor (DSIF) and negative elongation factor (NELF). Here we report the cryo-electron microscopy (cryo-EM) structure of the paused Sus scrofa/Homo sapiens Pol II-DSIF-NELF transcription elongation complex (PEC) at 3.2 Å resolution. The structure reveals a tilted DNA-RNA hybrid that impairs binding of the nucleoside triphosphate (NTP) substrate. NELF binds the polymerase funnel, bridges two mobile polymerase modules, and contacts the trigger loop, thereby restraining Pol II mobility that is required for pause release. NELF prevents binding of the anti-pausing factor TFIIS. Additionally, NELF possesses two flexible tentacles that can contact DSIF and exiting RNA. These results define the paused state of Pol II and provide the molecular basis for understanding NELF function during promoter-proximal gene regulation.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              A pause sequence enriched at translation start sites drives transcription dynamics in vivo.

              Transcription by RNA polymerase (RNAP) is interrupted by pauses that play diverse regulatory roles. Although individual pauses have been studied in vitro, the determinants of pauses in vivo and their distribution throughout the bacterial genome remain unknown. Using nascent transcript sequencing, we identified a 16-nucleotide consensus pause sequence in Escherichia coli that accounts for known regulatory pause sites as well as ~20,000 new in vivo pause sites. In vitro single-molecule and ensemble analyses demonstrate that these pauses result from RNAP-nucleic acid interactions that inhibit next-nucleotide addition. The consensus sequence also leads to pausing by RNAPs from diverse lineages and is enriched at translation start sites in both E. coli and Bacillus subtilis. Our results thus reveal a conserved mechanism unifying known and newly identified pause events. Copyright © 2014, American Association for the Advancement of Science.
                Bookmark

                Author and article information

                Contributors
                Role: Editor
                Journal
                mBio
                MBio
                mbio
                mbio
                mBio
                mBio
                American Society for Microbiology (1752 N St., N.W., Washington, DC )
                2150-7511
                26 February 2019
                Jan-Feb 2019
                : 10
                : 1
                : e01547-18
                Affiliations
                [a ]Department of Microbiology and The Center for RNA Biology, The Ohio State University, Columbus, Ohio, USA
                [b ]Lehrstuhl Biopolymere, Universität Bayreuth, Bayreuth, Germany
                University of Texas Health Science Center at Houston
                Author notes
                Address correspondence to Irina Artsimovitch, artsimovitch.1@ 123456osu.edu .
                Author information
                https://orcid.org/0000-0002-8604-0980
                https://orcid.org/0000-0002-4143-0694
                Article
                mBio01547-18
                10.1128/mBio.01547-18
                6391919
                30808693
                5d3a62ee-fde4-409e-9ef4-f4823ea02705
                Copyright © 2019 Artsimovitch and Knauer.

                This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.

                History
                Page count
                Figures: 4, Tables: 1, Equations: 0, References: 126, Pages: 16, Words: 10876
                Funding
                Funded by: HHS | National Institutes of Health (NIH), https://doi.org/10.13039/100000002;
                Award ID: GM67153
                Award Recipient :
                Categories
                Minireview
                Molecular Biology and Physiology
                Custom metadata
                January/February 2019

                Life sciences
                nusg,rfah,antitermination,transcription,translation
                Life sciences
                nusg, rfah, antitermination, transcription, translation

                Comments

                Comment on this article