title: What is the structure of the RecA-DNA filament?
abstract: The bacterial RecA protein has been a model system for understanding how a protein can catalyze homologous genetic recombination. RecA-like proteins have now been characterized from many organisms, from bacteriophage to humans. Some of the RecA-like proteins, including human RAD51, appear to function as helical filaments formed on DNA. However, we currently have high resolution structures of inactive forms of the protein, and low resolution structures of the active complexes formed by RecA-like proteins on DNA in the presence of ATP or ATP analogs. Within a crystal of the E. coli RecA protein, a helical polymer exists, and it has been widely assumed that this polymer is quite similar to the active helical filament formed on DNA. Recent developments have suggested that this may not be the case.
authors.affiliation: Department of Biochemistry, University of Virginia Health Sciences Center, Charlottesville VA 22908-0733, USA.
authors.forename: X
authors.initials: X
authors.lastname: Yu
authors.forename: M S
authors.initials: MS
authors.lastname: VanLoock
authors.forename: S
authors.initials: S
authors.lastname: Yang
authors.forename: J T
authors.initials: JT
authors.lastname: Reese
authors.forename: E H
authors.initials: EH
authors.lastname: Egelman
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000648:ultrastructure; D000255:Adenosine Triphosphate / Q000737:chemistry*; D000818:Animals; D019843:Archaeal Proteins / Q000737:chemistry; D024682:BRCA2 Protein / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry* / Q000648:ultrastructure; D004265:DNA Helicases / Q000737:chemistry / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000737:chemistry; D006801:Humans; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry; D008854:Microscopy, Electron; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D051135:Rad51 Recombinase; D011938:Rec A Recombinases / Q000737:chemistry* / Q000648:ultrastructure; D012234:Rho Factor / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry; D040681:Structural Homology, Protein; D014764:Viral Proteins / Q000737:chemistry; D000099160:LexA Repressor Protein
chemical_list: D000251:Adenosine Triphosphatases; D000255:Adenosine Triphosphate; D019843:Archaeal Proteins; D024682:BRCA2 Protein; D001426:Bacterial Proteins; D004247:DNA; D004265:DNA Helicases; D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D008565:Membrane Proteins; D051135:Rad51 Recombinase; D011938:Rec A Recombinases; D012234:Rho Factor; D012697:Serine Endopeptidases; D014764:Viral Proteins; D000099160:LexA Repressor Protein; C117252:RadA protein, archaeal; C092863:UvsX protein, Enterobacteria phage T4; C495153:RAD51 protein, human