DNA replication defects in a mutant deficient in the thioredoxin homolog YbbN
| Autor: | Gilbert Richarme, Hai Tuong Le, Masamichi Kohiyama, Tsutomu Katayama, Fatoum Kthiri, Valérie Gautier |
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| Přispěvatelé: | Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Department of Molecular Biology, Graduate School of Pharmaceutical Sciences, Kyushu University, Kyushu University [Fukuoka] |
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
DNA Replication
Protein Denaturation MESH: Microscopy MESH: Mutation DNA polymerase DNA polymerase II MESH: DNA Polymerase III Biophysics Eukaryotic DNA replication MESH: DNA Replication MESH: Escherichia coli Proteins MESH: Flow Cytometry Chaperone Biochemistry DNA polymerase delta 03 medical and health sciences Thioredoxins MESH: Thioredoxins Control of chromosome duplication Escherichia coli Urea Oxidoreductases Acting on Sulfur Group Donors Thioredoxin Molecular Biology MESH: Urea 030304 developmental biology DNA Polymerase III 0303 health sciences Microscopy DNA clamp biology MESH: Escherichia coli Escherichia coli Proteins 030302 biochemistry & molecular biology DNA replication [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Cell Biology Flow Cytometry Molecular biology Oxidoreductase Mutation biology.protein MESH: Protein Denaturation DNA polymerase I MESH: Molecular Chaperones MESH: Oxidoreductases Acting on Sulfur Group Donors Molecular Chaperones β-clamp |
| Zdroj: | Biochemical and Biophysical Research Communications Biochemical and Biophysical Research Communications, Elsevier, 2011, 405 (1), pp.52-7. ⟨10.1016/j.bbrc.2010.12.122⟩ |
| ISSN: | 0006-291X 1090-2104 |
| DOI: | 10.1016/j.bbrc.2010.12.122⟩ |
| Popis: | International audience; Escherichia coli contains two thioredoxins, Trx1 and Trx2, and a thioredoxin-like protein, YbbN, that displays both redox and chaperone properties. Since three out of the six proteins of the YbbN interactome (Butland et al., 2005) are components of DNA polymerase 3 holoenzyme (i.e. the β-clamp DnaN, the θ subunit HolE and the δ' subunit HolB), we investigated whether the ybbN mutant presents DNA replication defects. We found that this mutant incorporates (3)H-thymidine at higher rates than the parental strain and displays overinitiation, hypermutator and filamentation phenotypes with the occurrence of anucleated cells. Moreover, YbbN functions as a bona fide chaperone in the refolding of the urea-unfolded β-clamp. These results suggest that the DNA replication and cell division defects of the ybbN mutant might best be explained by chaperone functions of YbbN in the biogenesis of DNA polymerase 3 holoenzyme. |
| Databáze: | OpenAIRE |
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