‘Drc’, a structurally novel ssDNA-binding transcription regulator of N4-related bacterial viruses
| Autor: | De Zitter, Elke, Boon, Maarten, De Smet, Jeroen, Wagemans, Jeroen, Voet, Marleen, Pennemann, Friederike, Schalck, Thomas, Kuznedelov, Konstantin, Severinov, Konstantin, Van Meervelt, Luc, De Maeyer, Marc, Lavigne, Rob |
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| Přispěvatelé: | Groupe Dynamique et Cinétique des processus moléculaires (IBS-DYNAMOP), Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Department of Biosystems (BIOSYST), Catholic University of Leuven - Katholieke Universiteit Leuven (KU Leuven), Department of Chemistry [Leuven], Waksman Institute of Microbiology [Piscataway, NJ], Rutgers, The State University of New Jersey [New Brunswick] (RU), Rutgers University System (Rutgers)-Rutgers University System (Rutgers), European Project: 819800,BIONICbacteria, Groupe Dynamique et Cinétique des processus moléculaires (IBS-DYNAMOP ), Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA) |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular Protein Conformation alpha-Helical [SDV.BIO]Life Sciences [q-bio]/Biotechnology Transcription Genetic PROTEIN Gene Expression chemistry.chemical_compound DOMAIN Transcription (biology) STRANDS Structural Biology RNA polymerase Gene expression Cloning Molecular PC4 Promoter Regions Genetic Genetics 0303 health sciences COACTIVATOR [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] 030302 biochemistry & molecular biology DNA-Directed RNA Polymerases Recombinant Proteins DNA-Binding Proteins ALIGNMENT Pseudomonas Phages Life Sciences & Biomedicine Protein Binding Biochemistry & Molecular Biology DNA-BINDING Genetic Vectors DNA Single-Stranded PHAGE RNA polymerase complex Biology SEQUENCE 03 medical and health sciences Open Reading Frames Viral Proteins Pseudomonas Escherichia coli Protein Interaction Domains and Motifs Amino Acid Sequence Gene 030304 developmental biology Science & Technology Binding Sites Promoter chemistry Amino Acid Substitution DNA Viral Nucleic Acid Conformation Protein Conformation beta-Strand Bacterial virus Protein Multimerization DNA GENERATION |
| Zdroj: | Nucleic Acids Research Nucleic Acids Research, Oxford University Press, 2019, ⟨10.1093/nar/gkz1048⟩ Nucleic Acids Research, 2019, 48 (1), pp.445-459. ⟨10.1093/nar/gkz1048⟩ |
| ISSN: | 0305-1048 1362-4962 |
| Popis: | Bacterial viruses encode a vast number of ORFan genes that lack similarity to any other known proteins. Here, we present a 2.20 Å crystal structure of N4-related Pseudomonas virus LUZ7 ORFan gp14, and elucidate its function. We demonstrate that gp14, termed here as Drc (ssDNA-binding RNA Polymerase Cofactor), preferentially binds single-stranded DNA, yet contains a structural fold distinct from other ssDNA-binding proteins (SSBs). By comparison with other SSB folds and creation of truncation and amino acid substitution mutants, we provide the first evidence for the binding mechanism of this unique fold. From a biological perspective, Drc interacts with the phage-encoded RNA Polymerase complex (RNAPII), implying a functional role as an SSB required for the transition from early to middle gene transcription during phage infection. Similar to the coliphage N4 gp2 protein, Drc likely binds locally unwound middle promoters and recruits the phage RNA polymerase. However, unlike gp2, Drc does not seem to need an additional cofactor for promoter melting. A comparison among N4-related phage genera highlights the evolutionary diversity of SSB proteins in an otherwise conserved transcription regulation mechanism. ispartof: NUCLEIC ACIDS RESEARCH vol:48 issue:1 pages:445-459 ispartof: location:England status: published |
| Databáze: | OpenAIRE |
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