Výsledky vyhledávání

Ribosomal protein S1 and NusA protein complexed to recombination protein beta of phage lambda

Autor: C M Radding, T V Venkatesh

Publikováno v: Journal of Bacteriology. 175:1844-1846

The red genes of bacteriophage lambda specify two proteins, exonuclease and beta protein, which are essential for general recombination of lambda in recA cells. Earlier studies suggested that these proteins form an equimolar complex (C. M. Radding, J

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e663d62f3f59b108972e4b7d6d4bd5c
https://doi.org/10.1128/jb.175.6.1844-1846.1993

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Kinetic analysis of pairing and strand exchange catalyzed by RecA. Detection by fluorescence energy transfer

Autor: L R, Bazemore, M, Takahashi, C M, Radding

Publikováno v: The Journal of biological chemistry. 272(23)

RecA is a 38-kDa protein from Escherichia coli that polymerizes on single-stranded DNA, forming a nucleoprotein filament that pairs with homologous duplex DNA and carries out strand exchange in vitro. In this study, we measured RecA-catalyzed pairing

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ce507b6b9724afa05004530de803bc36
https://pubmed.ncbi.nlm.nih.gov/9169430

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A possible role of the C-terminal domain of the RecA protein. A gateway model for double-stranded DNA binding

Autor: H, Kurumizaka, H, Aihara, S, Ikawa, T, Kashima, L R, Bazemore, K, Kawasaki, A, Sarai, C M, Radding, T, Shibata

Publikováno v: The Journal of biological chemistry. 271(52)

According to the crystal structure, the RecA protein has a domain near the C terminus consisting of amino acid residues 270-328 (from the N terminus). Our model building pointed out the possibility that this domain is a part of "gateway" through whic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e5ca7043ed56ebf91749c4e51c97c582
https://pubmed.ncbi.nlm.nih.gov/8969216

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RecA protein mediates homologous recognition via non-Watson-Crick bonds in base triplets

Autor: C. M. Radding, B. J. Rao

Publikováno v: Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 347(1319)

E. coli RecA protein, the prototype of a class, forms a helical nucleoprotein filament on single-stranded DNA that recognizes homology in duplex DNA, and initiates the exchange of strands in homologous recombination. The discovery of this reaction so

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8c5bf3d87de103a632c663648714a68
https://pubmed.ncbi.nlm.nih.gov/7746854

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RecA protein mediates homologous recognition via non-Watson-Crick bonds in base triplets

Autor: B. J. Rao, C. M. Radding

Publikováno v: DNA Repair and Recombination ISBN: 9789401042390

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ed9e0d78b5067bb58f6e9393dfd29e04
https://doi.org/10.1007/978-94-011-0537-8_1

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Resolution of the three-stranded recombination intermediate made by RecA protein. An essential role of ATP hydrolysis

Autor: B, Burnett, B J, Rao, B, Jwang, G, Reddy, C M, Radding

Publikováno v: Journal of molecular biology. 238(4)

Previous work has shown that triplex DNA is an intermediate in homologous pairing and strand exchange promoted by RecA protein. Heterology at the proximal end of duplex DNA blocks strand exchange, but triplex joints form nonetheless at the homologous

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::21752f1e1bef2994067c10d506b02030
https://pubmed.ncbi.nlm.nih.gov/8176744

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Homologous recombination: a universal recombination filament

Autor: C M, Radding

Publikováno v: Current biology : CB. 3(6)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f4269872a388ef8434b125cf198ce7d9
https://pubmed.ncbi.nlm.nih.gov/15335730

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Helical interactions in homologous pairing and strand exchange driven by RecA protein

Autor: C M, Radding

Publikováno v: The Journal of biological chemistry. 266(9)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5b1a16167bb5fe66f7fbad0e8420b6b7
https://pubmed.ncbi.nlm.nih.gov/2005084

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RecA protein reinitiates strand exchange on isolated protein-free DNA intermediates. An ADP-resistant process

Autor: B J, Rao, B, Jwang, C M, Radding

Publikováno v: Journal of molecular biology. 213(4)

Efficient homologous pairing de novo of linear duplex DNA with a circular single strand (plus strand) coated with RecA protein requires saturation and extension of the single strand by the protein. However, strand exchange, the transfer of a strand f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0e88e9e4ab8c588e098821c3b959df9a
https://pubmed.ncbi.nlm.nih.gov/2141651

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Escherichia coli recA protein protects single-stranded DNA or gapped duplex DNA from degradation by RecBC DNase

Autor: J G Williams, C M Radding, Takehiko Shibata

Publikováno v: Journal of Biological Chemistry. 256:7573-7582

RecA- mutants of Escherichia coli extensively degrade their DNA following UV irradiation. Most of this degradation is due to the recBC DNase, which suggests that the recA gene is involved in the control of recBC DNase in vivo. We have shown that puri

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f4cce5f36ec43ae6b3fa1c6f1de405fc
https://doi.org/10.1016/s0021-9258(19)69000-9

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