ArticleJournal of bacteriology1996
Evolutionary conservation of RecA genes in relation to protein structure and function.
Article in Journal of bacteriology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 144 citations in OpenAlex.
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- Homology recognition without double-stranded DNA-strand separation in D-loop formation by RecA.Nucleic acids research · 2024Article
- Evolutionary conservation of sequence motifs at sites of protein modification.The Journal of biological chemistry · 2023Article
- Identification of amino acid domains ofFrontiers in cellular and infection microbiology · 2022Article
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- In vitro role of Rad54 in Rad51-ssDNA filament-dependent homology search and synaptic complexes formation.Nature communications · 2019Article
- Human NK cell receptor KIR2DS4 detects a conserved bacterial epitope presented by HLA-C.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- SOS Response Inhibitory Properties by Potential Probiotic Formulations of Bacillus amyloliquefaciens B-1895 and Bacillus subtilis KATMIRA1933 Obtained by Solid-State Fermentation.Current microbiology · 2019Article
- Exploring the rearrangement of sensory intelligence in proteobacteria: insight of Pho regulon.World journal of microbiology & biotechnology · 2018Article
- The Use of Biosensors to Explore the Potential of Probiotic Strains to Reduce the SOS Response and Mutagenesis in Bacteria.Biosensors · 2018Article
- Uncovering missing pieces: duplication and deletion history of arrestins in deuterostomes.BMC evolutionary biology · 2017Article
- Predicting Protein-Protein Interaction Sites Using Sequence Descriptors and Site Propensity of Neighboring Amino Acids.International journal of molecular sciences · 2016Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Functional and structural regions inferred from the Escherichia coli R ecA protein crystal structure and mutation studies are evaluated in terms of evolutionary conservation across 63 RecA eubacterial sequences. Two paramount segments invariant in specific amino acids correspond to the ATP-binding A site and the functionally unassigned segment from residues 145 to 149 immediately carboxyl to the ATP hydrolysis B site. Not only are residues 145 to 149 conserved individually, but also all three-dimensional structural neighbors of these residues are invariant, strongly attesting to the functional or structural importance of this segment. The conservation of charged residues at the monomer-monomer interface, emphasizing basic residues on one surface and acidic residues on the other, suggests that RecA monomer polymerization is substantially mediated by electrostatic interactions. Different patterns of conservation also allow determination of regions proposed to interact with DNA, of LexA binding sites, and of filament-filament contact regions. Amino acid conservation is also compared with activities and properties of certain RecA protein mutants. Arginine 243 and its strongly cationic structural environment are proposed as the major site of competition for DNA and LexA binding to RecA. The conserved acidic and glycine residues of the disordered loop L1 and its proximity to the RecA acidic monomer interface suggest its involvement in monomer-monomer interactions rather than DNA binding. The conservation of various RecA positions and regions suggests a model for RecA-double-stranded DNA interaction and other functional and structural assignments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.