THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN
- THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN
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Byrne, RT; Klingele, AJ; Cabot, EL; Schackwitz, WS; Martin, JA; Martin, J; Wang, Z; Wood, EA; Pennacchio, C; Pennacchio, LA; Perna, NT; Battista, JR; Cox, MM (2014)
Projects: NIH | THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN (2R01GM032335-04)eLife digest X-rays and other forms of ionizing radiation can damage DNA and proteins inside cells. The radiation interacts with aqueous solutions to produce reactive forms of oxygen, which then cause the damage. A range of mechanisms exist to moderate and/or repair this damage, with certain species being able to tolerate extraordinary levels of radiation. The bacterium D. radiodurans, for example, can survive radiation levels that are over 1000 times higher than the levels that can kill huma...
Developing Single-Molecule TPM Experiments for Direct Observation of Successful RecA-Mediated Strand Exchange ReactionFan, Hsiu-Fang; Cox, Michael M.; Li, Hung-Wen (2011)
Projects: NIH | THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN (2R01GM032335-04)RecA recombinases play a central role in homologous recombination. Once assembled on single-stranded (ss) DNA, RecA nucleoprotein filaments mediate the pairing of homologous DNA sequences and strand exchange processes. We have designed two experiments based on tethered particle motion (TPM) to investigate the fates of the invading and the outgoing strands during E. coli RecA-mediated pairing and strand exchange at the single-molecule level in the absence of force. TPM experiments measure the ...Irina V Bakhlanova; Alexandra V Dudkina; Elizabeth A Wood; Vladislav A Lanzov; Michael M Cox; Dmitry M Baitin
Projects: NIH | THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN (2R01GM032335-04)The RecA recombinase of Escherichia coli has not evolved to optimally promote DNA pairing and strand exchange, the key processes of recombinational DNA repair. Instead, the recombinase function of RecA protein represents an evolutionary compromise between necessary levels of recombinational DNA repair and the potentially deleterious consequences of RecA functionality. A RecA variant, RecA D112R, promotes conjugational recombination at substantially enhanced levels. However, expression of the ...
The Deinococcus radiodurans DR1245 Protein, a DdrB Partner Homologous to YbjN Proteins and Reminiscent of Type III Secretion System ChaperonesNorais, Cédric; Servant, Pascale; Bouthier-de-la-Tour, Claire; Coureux, Pierre-Damien; Ithurbide, Solenne; Vannier, Françoise; Guerin, Philippe P.; Dulberger, Charles L.; Satyshur, Kenneth A.; Keck, James L.; Armengaud, Jean; Cox, Michael M.; Sommer, Suzanne (2013)
Projects: NIH | THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN (2R01GM032335-04), NIH | Structure and Function of Bacterial RecQ Protein (5R01GM068061-05)The bacterium Deinococcus radiodurans exhibits an extreme resistance to ionizing radiation. A small subset of Deinococcus genus-specific genes were shown to be up-regulated upon exposure to ionizing radiation and to play a role in genome reconstitution. These genes include an SSB-like protein called DdrB. Here, we identified a novel protein encoded by the dr1245 gene as an interacting partner of DdrB. A strain devoid of the DR1245 protein is impaired in growth, exhibiting a generation time ap...
Structural and Functional Studies of H. seropedicae RecA Protein – Insights into the Polymerization of RecA Protein as Nucleoprotein FilamentLeite, Wellington C.; Galvão, Carolina W.; Saab, Sérgio C.; Iulek, Jorge; Etto, Rafael M.; Steffens, Maria B. R.; Chitteni-Pattu, Sindhu; Stanage, Tyler; Keck, James L.; Cox, Michael M. (2016)
Projects: NIH | THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN (2R01GM032335-04), NIH | Structure and function of the bacterial primosome (1R01GM098885-01A1)The bacterial RecA protein plays a role in the complex system of DNA damage repair. Here, we report the functional and structural characterization of the Herbaspirillum seropedicae RecA protein (HsRecA). HsRecA protein is more efficient at displacing SSB protein from ssDNA than Escherichia coli RecA protein. HsRecA also promotes DNA strand exchange more efficiently. The three dimensional structure of HsRecA-ADP/ATP complex has been solved to 1.7 Å resolution. HsRecA protein contains a small N...Gruber, Angela J.; Olsen, Tayla M.; Dvorak, Rachel H.; Cox, Michael M. (2015)
Projects: NIH | THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN (2R01GM032335-04), NIH | Graduate Training in Molecular Biosciences (2T32GM007215-36)The bacteriophage P1 Ref (recombination enhancement function) protein is a RecA-dependent, HNH endonuclease. It can be directed to create targeted double-strand breaks within a displacement loop formed by RecA. The 76 amino acid N-terminal region of Ref is positively charged (25/76 amino acid residues) and inherently unstructured in solution. Our investigation of N-terminal truncation variants shows this region is required for DNA binding, contains a Cys involved in incidental dimerization an...Lewis, J.; Spenkelink, L.; Jergic, S.; Wood, E.; Monachino, E.; Horan, N.; Duderstadt, K.; Cox, M.; Robinson, A.; Dixon, N.; van Oijen, A. (2017)
Projects: ARC | Australian Laureate Fellowships - Grant ID: FL140100027 (FL140100027), ARC | Discovery Projects - Grant ID: DP150100956 (DP150100956), NIH | THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN (2R01GM032335-04)The Escherichia coli DNA replication machinery has been used as a road map to uncover design rules that enable DNA duplication with high efficiency and fidelity. Although the enzymatic activities of the replicative DNA Pol III are well understood, its dynamics within the replisome are not. Here, we test the accepted view that the Pol III holoenzyme remains stably associated within the replisome. We use in vitro single-molecule assays with fluorescently labeled polymerases to demonstrate that ...Henrikus, Sarah S.; Wood, Elizabeth A.; McDonald, John P.; Cox, Michael M.; Woodgate, Roger; Goodman, Myron F.; van Oijen, Antoine M.; Robinson, Andrew (2018)
Projects: NIH | THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN (2R01GM032335-04), NIH | Biochemical Basis of SOS-Induced Mutagenesis (5R01ES012259-18), ARC | Australian Laureate Fellowships - Grant ID: FL140100027 (FL140100027), NIH | Molecular Mechanisms of Human DNA Polymerase Beta Catalysis, Fidelity and Selective Inhibition (5U19CA177547-03)In Escherichia coli, damage to the chromosomal DNA induces the SOS response, setting in motion a series of different DNA repair and damage tolerance pathways. DNA polymerase IV (pol IV) is one of three specialised DNA polymerases called into action during the SOS response to help cells tolerate certain types of DNA damage. The canonical view in the field is that pol IV primarily acts at replisomes that have stalled on the damaged DNA template. However, the results of several studies indicate ...Stohl, Elizabeth A.; Gruenig, Marielle C.; Cox, Michael M.; Seifert, H. Steven (2011)
Projects: NIH | Molecular genetics of the gonococcus (5R01AI044239-09), NIH | MECHANISMS OF GONOCOCCAL PILIN ANTIGENIC/PHASE VARIATION (5R01AI033493-07), HRZZ | Energy efficient asynchronous wireless transmission (6219), NIH | THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN (2R01GM032335-04)The strict human pathogen Neisseria gonorrhoeae is the only causative agent of the sexually transmitted infection gonorrhea. The recA gene from N. gonorrhoeae is essential for DNA repair, natural DNA transformation, and pilin antigenic variation, all processes that are important for the pathogenesis and persistence of N. gonorrhoeae in the human population. To understand the biochemical features of N. gonorrhoeae RecA (RecA(Ng)), we overexpressed and purified the RecA(Ng) and SSB(Ng) proteins...Ronayne, Erin A.; Cox, Michael M. (2013)
Projects: NIH | Graduate Training in Molecular Biosciences (2T32GM007215-36), NIH | THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEIN (2R01GM032335-04), NSF | Graduate Reserach Fellowship Program (GRFP) (1256259)The bacteriophage P1 recombination enhancement function (Ref) protein is a RecA-dependent programmable endonuclease. Ref targets displacement loops formed when an oligonucleotide is bound by a RecA filament and invades homologous double-stranded DNA sequences. Mechanistic details of this reaction have been explored, revealing that (i) Ref is nickase, cleaving the two target strands of a displacement loop sequentially, (ii) the two strands are cleaved in a prescribed order, with the paired str...
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