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Rad51 and RecA juxtapose dsDNA ends ready for DNA ligase-catalyzed end-joining under recombinase-suppressive conditions

RecA-family recombinase-catalyzed ATP-dependent homologous joint formation is critical for homologous recombination, in which RecA or Rad51 binds first to single-stranded (ss)DNA and then interacts with double-stranded (ds)DNA. However, when RecA or Rad51 interacts with dsDNA before binding to ssDNA, the homologous joint-forming activity of RecA or Rad51 is quickly suppressed. We...

Loop L1 governs the DNA-binding specificity and order for RecA-catalyzed reactions in homologous recombination and DNA repair

In all organisms, RecA-family recombinases catalyze homologous joint formation in homologous genetic recombination, which is essential for genome stability and diversification. In homologous joint formation, ATP-bound RecA/Rad51-recombinases first bind single-stranded DNA at its primary site and then interact with double-stranded DNA at another site. The underlying reason and the...

Homologous Pairing Activities of Two Rice RAD51 Proteins, RAD51A1 and RAD51A2

In higher eukaryotes, RAD51 functions as an essential protein in homologous recombination and recombinational repair of DNA double strand breaks. During these processes, RAD51 catalyzes homologous pairing between single-stranded DNA and double-stranded DNA. Japonica cultivars of rice (Oryza sativa) encode two RAD51 proteins, RAD51A1 and RAD51A2, whereas only one RAD51 exists in...

The process of displacing the single-stranded DNA-binding protein from single-stranded DNA by RecO and RecR proteins

Jin Inoue Masayoshi Honda Shukuko Ikawa Takehiko Shibata Tsutomu Mikawa The regions of single-stranded (ss) DNA that result from DNA damage are immediately coated by the ssDNA-binding protein (SSB

Filament formation and robust strand exchange activities of the rice DMC1A and DMC1B proteins

The DMC1 protein, a meiosis-specific DNA recombinase, catalyzes strand exchange between homologous chromosomes. In rice, two Dmc1 genes, Dmc1A and Dmc1B, have been reported. Although the Oryza sativa DMC1A protein has been partially characterized, however the biochemical properties of the DMC1B protein have not been defined. In the present study, we expressed the Oryza sativa...

Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein

Naoyuki Sarai Wataru Kagawa Takashi Kinebuchi Ako Kagawa Kozo Tanaka Kiyoshi Miyagawa Shukuko Ikawa Takehiko Shibata Hitoshi Kurumizaka Shigeyuki Yokoyama The process of homologous recombination is

Structural and functional analyses of the DMC1-M200V polymorphism found in the human population

Juri Hikiba Kouji Hirota Wataru Kagawa Shukuko Ikawa Takashi Kinebuchi Isao Sakane Yoshimasa Takizawa Shigeyuki Yokoyama B eatrice Mandon-Pe pin Alain Nicolas Takehiko Shibata Kunihiro Ohta Hitoshi

Imaging the RecA-DNA complex by atomic force microscopy

Kazuo Umemura 1 Shukuko Ikawa Taro Nishinaka Takehiko Shibata Reiko Kuroda 0 Graduate School of Arts and Sciences, The University of Tokyo , Komaba, Meguro-ku, Tokyo 153-8902, Japan 1 Joint Research

RecA-double stranded DNA complexes studied by atomic force microscopy

RecA-double stranded (ds) DNA complexes have been studied by atomic force microscopy(AFM). When the complexes were prepared in the presence of ATPĪ³S, fully covered RecA-dsDNA filaments were observed by AFM. When the concentration of RecA proteins was lower, various lengths of filaments were found. The variation of the observed structures may directly reflect the real distribution...