DNA replication defects in a mutant deficient in the thioredoxin homolog YbbN

Biochemical and Biophysical Research Communications
Hai-Tuong LeGilbert Richarme


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.


Mar 11, 2020·Infection and Immunity·Sadia SultanaJan-Ulrik Dahl


Jan 10, 1998·The Journal of Biological Chemistry·A Miranda-VizueteG Spyrou
Sep 30, 2000·European Journal of Biochemistry·E S Arnér, Arne Holmgren
Jan 29, 2003·The Biochemical Journal·Renée KernGilbert Richarme
Sep 1, 2005·Molecular Genetics and Genomics : MGG·Shun AdachiSota Hiraga
Jan 20, 2006·The Journal of Biological Chemistry·Mike O'Donnell
Mar 12, 2008·Biochimica Et Biophysica Acta·Carsten BerndtArne Holmgren

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