Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
RecFOR proteins in homologous recombinationSato, Katsuya; Kikuchi, Masahiro; Ishaque, A. M.*; Oba, Hirofumi*; Yamada, Mitsugu; Tejima, Kohei; Onodera, Takefumi; Narumi, Issei
DNA Repair, 11(4), p.410 - 418, 2012/04
Times Cited Count：24 Percentile：59.62(Genetics & Heredity)In an effort to gain insights into the role of 
RecFOR proteins in homologous recombination, we generated 
, 
and 
disruptant strains and characterized the disruption effects. Disruption of resulted in severe reduction of the transformation efficiency. On the other hand, the disruptant strain was the most sensitive phenotype to 
rays, UV irradiation and mitomycin C among the three disruptants. In the disruptant strain, the intracellular level of the LexA1 protein did not decrease following irradiation. These results demonstrate that the RecF protein plays a crucial role in the homologous recombination repair process by facilitating RecA activation. Thus, the RecF and RecR proteins are involved in the RecA activation and the stability of incoming DNA, respectively, during RecA-mediated homologous recombination processes that initiated the ESDSA pathway in .
Sakamoto, Ayako; Stone, J. E.*; Kissling, G. E.*; McCulloch, S. D.*; Pavlof, Y. I.*; Kunkel, T. A.*
DNA Repair, 6(12), p.1829 - 1838, 2007/12
no abstracts in English
SOS-regulated UmuD
proteinSutton, M. D.*; Guzzo, A.*; Narumi, Issei; Costanzo, M.*; Altenbach, C.*; Ferentz, A. E.*; Hubbell, W. L.*; Walker, G. C.*
DNA Repair, 1(1), p.77 - 93, 2002/01
UmuD protein is a regulatory subunit of DNA polymerase V. This protein forms a complex with UmuC protein, a catalytic subunit of DNA polymerase V, and plays a important role in error-prone translesion DNA synthesis, which serves as the mechanistic basis for most DNA-damaging agent and UV light mutagenesis. In this paper, based on the results of a combination of experimental studies, we have developed a refined model for the structure of the UmuD homodimer. Implications of the structural change of UmuD protein with respect to its roles in managing the action of DNA polymease V are discussed.
mutantKiyosawa, Kazuhiro*; Tanaka, Masashi*; Matsunaga, Tsukasa*; Nikaido, Osamu*; Yamamoto, Kazuo
Mutation Research; DNA Repair, 487(3-4), p.149 - 156, 2001/12
no abstracts in English
Kitayama, Shigeru*; Narumi, Issei; Kikuchi, Masahiro; Watanabe, Hiroshi
Mutation Research; DNA Repair, 461(3), p.179 - 187, 2000/11
no abstracts in English
Funayama, Tomoo; Narumi, Issei; Kikuchi, Masahiro; Kitayama, Shigeru*; Watanabe, Hiroshi; Yamamoto, Kazuo
Mutation Research; DNA Repair, 435, p.151 - 161, 1999/00
no abstracts in English
Narumi, Issei; Sato, Katsuya; Kikuchi, Masahiro; Funayama, Tomoo; Kitayama, Shigeru; Yanagisawa, Tadashi*; Watanabe, Hiroshi; Yamamoto, Kazuo
Mutation Research; DNA Repair, 435(3), p.233 - 243, 1999/00
no abstracts in English
Shikazono, Naoya; Watanabe, Hiroshi; ; Tano, Shigemitsu*; *; *
Mutat. Res., DNA Repair, 337, p.41 - 48, 1995/00
no abstracts in English
