Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Katsumi Morimatsu"'
Publikováno v:
Journal of Biological Chemistry. 287:35621-35630
The repair of single-stranded gaps in duplex DNA by homologous recombination requires the proteins of the RecF pathway. The assembly of RecA protein onto gapped DNA (gDNA) that is complexed with the single-stranded DNA-binding protein is accelerated
Publikováno v:
Genes & Development. 23:1234-1245
The RecF pathway of Escherichia coli is important for recombinational repair of DNA breaks and gaps. Here `we reconstitute in vitro a seven-protein reaction that recapitulates early steps of dsDNA break repair using purified RecA, RecF, RecO, RecR, R
Autor:
Katsumi Morimatsu, Masayuki Takahashi
Publikováno v:
Analytical Biochemistry. 358:192-198
We have developed a simple measuring system for fluorescence-detected linear dichroism and applied it to the structural analysis of the RecA-DNA complex filaments, which are intermediates of the homologous recombination reaction. Taking advantage of
Publikováno v:
Molecular Cell. 11(5):1337-1347
Genetic evidence suggests that the RecF, RecO, and RecR (RecFOR) proteins participate in a common step of DNA recombination and repair, yet the biochemical event requiring collaboration of all three proteins is unknown. Here, we show that the concert
Publikováno v:
Genes to Cells. 7:1125-1134
Background: Human Rad51 protein (HsRad51) is a homologue of Escherichia coli RecA protein, and involved in homologous recombination. These eukaryotic and bacterial proteins catalyse strand exchange between two homologous DNA molecules, each forming a
Publikováno v:
Proceedings of the National Academy of Sciences. 99:11688-11693
Linear dichroism (LD) polarized-light spectroscopy is used to determine the arrangement of RecA in its large filamentous complex with DNA, active in homologous recombination. Angular orientation data for two tryptophan and seven tyrosine residues, de
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 111, iss 48
Recombinational DNA repair by the RecF pathway of Escherichia coli requires the coordinated activities of RecA, RecFOR, RecQ, RecJ, and single-strand DNA binding (SSB) proteins. These proteins facilitate formation of homologously paired joint molecul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ceb950c9a885f25de56de928a95ebda
https://europepmc.org/articles/PMC4260596/
https://europepmc.org/articles/PMC4260596/
Publikováno v:
Journal of Molecular Biology. 306:189-199
We investigated the structure of the active RecA-DNA complex by analyzing the environment of tyrosine residue 65, which is on the DNA-binding surface of the protein. We prepared a modified RecA protein in which the tyrosine residue was replaced by tr
Publikováno v:
Genes to Cells. 1:1057-1068
BACKGROUND: The RAD51 gene of Saccharomyces cerevisiae is homologous to the Escherichia coli recA gene and plays a key role in genetic recombination and DNA double-strand break repair. To construct an improved experimental system of homologous recomb
Publikováno v:
European Journal of Biochemistry. 228:779-785
To obtain structural insight on the interaction of the RecA protein with nucleotide cofactors (ATP and ADP) and DNA, we have made two engineered RecA proteins, in which either Tyr103 or Tyr264 was replaced with tryptophan. The fluorescence of tryptop