B. Li, P. Smith, D.J. Horvath, Jr, F.E. Romesberg, S.S. Justice, Microb. Infect. (2010) 12:662-668.
Epithelial cells are highly regarded as the first line of defense against microorganisms, but the mechanisms used to control bacterial diseases are poorly understood. A component of the DNA damage repair regulon, SulA, is essential for UPEC virulence in a mouse model for human urinary tract infection, suggesting that DNA damage is a key mediator in the primary control of pathogens within the epithelium. In this study, we examine the role of DNA damage repair regulators in the intracellular lifestyle of UPEC within superficial bladder epithelial cells.
E.T. Lis, B.M. O’Neill, C. Gil-Lemaignere, J.K. Chin, F.E. Romesberg, DNA Repair (2008) 7:801-810.
To further understand the mutagenic response to DNA damage, we screen a collection of 4848 haploid gene deletion strains of S. cerevisiae for decreased damage-induced mutation of the CAN1 gene, and we identify a pathway of induced mutation that involves a replicative polymerase and that is effectively inhibited by the RNR inhibitor, hydroxyurea.
J. Heideker, E.T. Lis, F.E. Romesberg, Cell Cycle (2007) 6:3058-3064.
We review progress toward understanding the functions of phosphatases in checkpoint deactivation in S. cerevisiae, focusing on the non-redundant roles of the type 2A phosphatase Pph3 and the PP2C phosphatases Ptc2 and Ptc3 in the deactivation of Rad53.
B.M. O’Neill, S.J. Szyjka, E.T. Lis, A.O. Bailey, J.R. Yates III, O.M. Aparicio, F.E. Romesberg, Proc. Natl. Acad. Sci. USA (2007) 104:9290-9295.
We present genetic and biochemical evidence that the type 2A-like protein phosphatase Pph3 forms a complex with Psy2 (Pph3–Psy2) that binds and dephosphorylates activated Rad53 during treatment with, and recovery from, methylmethane sulfonate-mediated DNA damage. Our findings suggest that Rad53 regulates replication fork restart and initiation of late firing origins independently and that regulation of these processes is mediated by specific Rad53 phosphatases order of magnitude relative to mispairing.
E.T. Lis, F.E. Romesberg, Mol. Cell. Biol. (2006) 26:4122-4133.
We show that the stability and selectivity of unnatural base pairs may be comparable to, or even exceed, that of native pairs and that the unnatural bases are orthogonal to the native bases, with correct pairing being favored by at least an order of magnitude relative to mispairing.
J.K. Chin, V.I. Bashkirov, W.-D. Heyer, F.E. Romesberg, DNA Repair (2006) 5:618-628.
We show that Esc4 interacts with several proteins involved in the repair and processing of stalled or collapsed replication forks, including the recombination protein Rad55, and we propose that Esc4 associates with ssDNA of stalled forks and acts as a scaffolding protein to recruit and/or modulate the function of other proteins required to reinitiate DNA synthesis.
B.M. O’Neill, D. Hanway, E.A. Winzeler, F.E. Romesberg, Nucleic Acids Res. (2004) 32:6519–6530.
The stabilization and processing of stalled replication forks is required to maintain genome integrity in all organisms. Based on both physical and genetic interactions detected between WSS1, PSY2, and TOF1, we suggest that Wss1 and Psy2 similarly function to stabilize or process stalled or collapsed replication forks.