Crystallization and preliminary X-ray crystallographic analysis of the RecR protein from<i>Deinococcus radiodurans</i>, a member of the RecFOR DNA-repair pathway

Lee, Byung Il; Kim, Kyoung Hoon; Shim, Sun Mi; Ha, Kyung Soo; Yang, Jong Oh; Yoon, Hye‐Jin; Ha, Jun Yong; Suh, Se Won

doi:10.1107/s0907444903028191

Cited by 5 publications

(3 citation statements)

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“…RecR molecules form a ring structure that can encircle both dsDNA and ssDNA [34],[35]. The structure of the RecF protein from D. radiodurans has also recently been elucidated, showing that the RecF protein exhibits extensive structural similarity with the head domain of the eukaryotic Rad50 protein [36].…”

Section: Discussionmentioning

confidence: 99%

A Major Role of the RecFOR Pathway in DNA Double-Strand-Break Repair through ESDSA in Deinococcus radiodurans

et al. 2010

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In Deinococcus radiodurans, the extreme resistance to DNA–shattering treatments such as ionizing radiation or desiccation is correlated with its ability to reconstruct a functional genome from hundreds of chromosomal fragments. The rapid reconstitution of an intact genome is thought to occur through an extended synthesis-dependent strand annealing process (ESDSA) followed by DNA recombination. Here, we investigated the role of key components of the RecF pathway in ESDSA in this organism naturally devoid of RecB and RecC proteins. We demonstrate that inactivation of RecJ exonuclease results in cell lethality, indicating that this protein plays a key role in genome maintenance. Cells devoid of RecF, RecO, or RecR proteins also display greatly impaired growth and an important lethal sectoring as bacteria devoid of RecA protein. Other aspects of the phenotype of recFOR knock-out mutants paralleled that of a ΔrecA mutant: ΔrecFOR mutants are extremely radiosensitive and show a slow assembly of radiation-induced chromosomal fragments, not accompanied by DNA synthesis, and reduced DNA degradation. Cells devoid of RecQ, the major helicase implicated in repair through the RecF pathway in E. coli, are resistant to γ-irradiation and have a wild-type DNA repair capacity as also shown for cells devoid of the RecD helicase; in contrast, ΔuvrD mutants show a markedly decreased radioresistance, an increased latent period in the kinetics of DNA double-strand-break repair, and a slow rate of fragment assembly correlated with a slow rate of DNA synthesis. Combining RecQ or RecD deficiency with UvrD deficiency did not significantly accentuate the phenotype of ΔuvrD mutants. In conclusion, RecFOR proteins are essential for DNA double-strand-break repair through ESDSA whereas RecJ protein is essential for cell viability and UvrD helicase might be involved in the processing of double stranded DNA ends and/or in the DNA synthesis step of ESDSA.

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Section: Discussionmentioning

confidence: 99%

A Major Role of the RecFOR Pathway in DNA Double-Strand-Break Repair through ESDSA in Deinococcus radiodurans

et al. 2010

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“…Recombinant DR RecR with a C‐terminal eight‐residue tag was overexpressed and crystallized as described elsewhere (Lee et al , 2004). The C‐terminal His 6 ‐tagged HP RecR was purified by the same procedure.…”

Section: Methodsmentioning

confidence: 99%

Ring-shaped architecture of RecR: implications for its role in homologous recombinational DNA repair

Lee

Kim

Park

et al. 2004

EMBO J

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108

139

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RecR, together with RecF and RecO, facilitates RecA loading in the RecF pathway of homologous recombinational DNA repair in procaryotes . The human Rad52 protein is a functional counterpart of RecFOR. We present here the crystal structure of RecR from Deinococcus radiodurans (DR RecR). A monomer of DR RecR has a two-domain structure: the N-terminal domain with a helix-hairpinhelix (HhH) motif and the C-terminal domain with a Cys 4 zinc-finger motif, a Toprim domain and a Walker B motif. Four such monomers form a ring-shaped tetramer of 222 symmetry with a central hole of 30À35 Å diameter. In the crystal, two tetramers are concatenated, implying that the RecR tetramer is capable of opening and closing. We also show that DR RecR binds to both dsDNA and ssDNA, and that its HhH motif is essential for DNA binding.

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“…The deletion of recN (6) and recQ (10) and the mutation of ruvB (14) result in the increased radiosensitivity of the mutant bacteria. The functions and structures of the pathway proteins RecA (12,13,27), RecF (16), RecO (21,23,31), RecR (19,20,31), and RecQ (9) were also investigated. However, little in vivo evidence has been presented to date for the roles of the unique genes recF, recO, and recR of the RecF pathway in D. radiodurans's radioresistance.…”

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confidence: 99%

RecO Is Essential for DNA Damage Repair in Deinococcus radiodurans

Wang

Chen

et al. 2008

J Bacteriol

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Crystallization and preliminary X-ray crystallographic analysis of the RecR protein fromDeinococcus radiodurans, a member of the RecFOR DNA-repair pathway

Cited by 5 publications

References 10 publications

A Major Role of the RecFOR Pathway in DNA Double-Strand-Break Repair through ESDSA in Deinococcus radiodurans

A Major Role of the RecFOR Pathway in DNA Double-Strand-Break Repair through ESDSA in Deinococcus radiodurans

Ring-shaped architecture of RecR: implications for its role in homologous recombinational DNA repair

RecO Is Essential for DNA Damage Repair in Deinococcus radiodurans

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