Does a stretched DNA structure dictate the helical geometry of RecA-like filaments?
Proteins in the RecA/Rad51/RadA/UvsX family form helical filaments on DNA in which the DNA is stretched and untwisted. A comparison of the average helical parameters of these filaments from five different proteins, obtained from archaea, eubacteria and eukaryotes, suggests that an intrinsic state of DNA may be responsible for the conservation of these particular filament forms across evolution. In this view, these proteins stabilize this existing state of DNA, rather than induce a novel conformation.
Egelman
E H
EH
Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733, USA. egelman@virginia.edu
D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D017122:Bacteriophage T4 / Q000737:chemistry; D001483:Base Sequence; D004247:DNA / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry; D019143:Evolution, Molecular; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D021122:Protein Subunits; D051135:Rad51 Recombinase; D011938:Rec A Recombinases / Q000737:chemistry* / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000737:chemistry; D029701:Saccharomyces cerevisiae Proteins; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism
D019843:Archaeal Proteins; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D008565:Membrane Proteins; D021122:Protein Subunits; C117252:RadA protein, archaeal; D029701:Saccharomyces cerevisiae Proteins; C092863:UvsX protein, Enterobacteria phage T4; D014764:Viral Proteins; D004247:DNA; C495151:RAD51 protein, S cerevisiae; C495153:RAD51 protein, human; D051135:Rad51 Recombinase; D011938:Rec A Recombinases