Journal of Molecular Biology
ArticleStructural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible☆
References (32)
- et al.
Cryo electron microscopy of unstained, Unfixed RecA-cssDNA complexes
J. Ultrastruct. Mol. Struct. Res
(1988) - et al.
Function of nucleoside triphosphate and polynucleotide in E. coli RecA protein-directed cleavage of phage lambda repressor
J. Biol. Chem
(1981) - et al.
Characterization of complexes bewteen RecA protein and duplex DNA by electron microscopy
J. Mol. Biol
(1982) - et al.
Complexes of RecA protein in solution. A study by small angle neutron scattering
J. Mol. Biol
(1990) - et al.
Structure of helical RecA-DNA complexes. Complexes formed in the presence of ATP-gamma-S or ATP
J. Mol. Biol
(1986) - et al.
Structure of helical RecA-DNA complexes. II. Local conformational changes visualized in bundles of RecA-ATPγS filaments
J. Mol. Biol
(1988) - et al.
Visualization of RecA protein and its complexes with DNA by quick-freeze/deep-etch electron microscopy
J. Mol. Biol
(1989) - et al.
The structure and dynamics of RecA protein-DNA complexes as determined by image analysis of electron micrographs
Biophys. J
(1986) - et al.
Elongation of duplex DNA by RecA protein
J. Mol. Biol
(1981) - et al.
Structure of helical RecA-DNA complexes. III. The structural polarity of RecA filaments and functional polarity in the RecA-mediated strand exchange reaction
J. Mol. Biol
(1988)
Binding stoiehiometry and structure of RecA-DNA complexes studied by flow linear dichroism and fluorescence spectroscopy. Evidence for multiple heterogeneous DNA co-ordination
J. Mol. Biol
Fibers of RecA protein and complexes of RecA protein and single-stranded φX174 DNA as visualized by negative-stain electron microscopy
J. Mol. Biol
Image analysis reveals that the E. coli RecA protein consists of two domains
Biophys. J
Removal of the RecA C-terminus results in a conformational change in the RecA-DNA filament
J. Struct. Biol
Direct visualization of dynamics and cooperative conformational changes within RecA flaments that appear to be associated with the hydrolysis of adenosine 5′-O-(3-thiotriphosphate)
J. Mol. Biol
Cited by (135)
Single-molecule characterization of compressed RecA nucleoprotein filaments
2022, Biochemical and Biophysical Research CommunicationsThe extended N-terminus of Mycobacterium smegmatis RecX potentiates its ability to antagonize RecA functions
2020, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :The electron microscopic [7,8] and crystallographic studies of E. coli RecA [9–11] together with high-resolution cryo-electron microscopy studies of Rad51 [12,13] have revealed a remarkably conserved structure of a RecA/Rad51 nucleoprotein filament [4–6]. The ssDNA in the nucleoprotein filament is extended 1.5-fold compared to the canonical B-form DNA with a binding stoichiometry of 3 nucleotides/RecA monomer [7,8,11]. The triplet in ssDNA serves as a fundamental unit of recognition of homology, pairing and strand exchange with homologous duplex DNA [4–6,11,14].
Cryo-EM: Ice Is Nice, but Good Ice Can Be Hard to Find
2020, Biophysical JournalCharacterization of the recombination activities of the Entamoeba histolytica Rad51 recombinase
2016, Molecular and Biochemical ParasitologyMismatch repair and homeologous recombination
2016, DNA RepairCitation Excerpt :RecA monomers cooperatively polymerize onto ssDNA to form a right-handed helix around the ssDNA with ATP cofactors bound between the monomers (Fig. 2A; [74,75]). The DNA in those filaments is approximately 150% of the length of corresponding B-form DNA [76–80]. RecA binds to the ssDNA with an exact stoichiometry of three nucleotides per RecA monomer (Fig. 2B).
Kinetics of the ATP and dATP-mediated formation of a functionally-active RecA-ssDNA complex
2015, Biochemical and Biophysical Research Communications
- ☆
This work was supported by NIH grant GM35269.