Distinct beta-clamp interactions govern the activities of the Y family PolIV DNA polymerase

Autor: Jérôme Wagner, Robert P. P. Fuchs, Hélène Etienne, Agnès M. Cordonnier, Dominique Burnouf
Přispěvatelé: CNRS FRE3211 (FRE3211), Centre National de la Recherche Scientifique (CNRS), Hôpital Civil, Strasbourg, Hopital Civil, Instabilité du génome et cancérogénèse (UPR3081), Architecture et Réactivité de l'ARN (ARN), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2009
Předmět:
DNA Replication
DNA
Bacterial
Models
Molecular
MESH: Mutation
DNA Repair
DNA polymerase
MESH: DNA Polymerase III
Cell
MESH: DNA Replication
[SDV.CAN]Life Sciences [q-bio]/Cancer
[SDV.BC]Life Sciences [q-bio]/Cellular Biology
medicine.disease_cause
Microbiology
Turn (biochemistry)
03 medical and health sciences
MESH: DNA Polymerase beta
Protein Interaction Mapping
medicine
Escherichia coli
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Protein Interaction Domains and Motifs
Molecular Biology
Polymerase
DNA Polymerase beta
030304 developmental biology
MESH: Mutagenesis
DNA Polymerase III
Genetics
MESH: DNA Repair
0303 health sciences
MESH: Protein Interaction Domains and Motifs
biology
MESH: Escherichia coli
030302 biochemistry & molecular biology
Mutagenesis
MESH: Protein Interaction Mapping
Sciences du Vivant [q-bio]/Biotechnologies
Nucleotidyltransferase
MESH: DNA
Bacterial
medicine.anatomical_structure
Mutation
biology.protein
Replisome
MESH: Models
Molecular
Zdroj: Molecular Microbiology
Molecular Microbiology, Wiley, 2009, 74 (5), pp.1143-51. ⟨10.1111/j.1365-2958.2009.06920.x⟩
ISSN: 1365-2958
0950-382X
DOI: 10.1111/j.1365-2958.2009.06920.x⟩
Popis: International audience; The prototypic Y family DNA polymerase IV (PolIV) of Escherichia coli is involved in multiple replication-associated processes including spontaneous mutagenesis, translesion synthesis (TLS), cell fitness, survival under stressful conditions and checkpoint like functions. It interacts physically and functionally with the replisome's beta processivity clamp through the canonical PolIV C-terminal peptide (CTP). A second interaction that involves a portion of the little finger (LF) domain of PolIV has been structurally described. Here we show that the LF-beta interaction stabilizes the clamp-polymerase complex in vitro and is necessary for the access of PolIV to ongoing replication forks in vivo. However, in contrast to the CTP-beta, the LF-beta interaction is dispensable for the role of the polymerase in TLS. This discloses two independent modes of action for PolIV and, in turn, uncovers a novel way by which the cell may regulate the potentially deleterious effect of such low fidelity polymerases during replication.
Databáze: OpenAIRE
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