RecA family proteins in archaea: RadA and its cousins

Haldenby, Sam; White, Malcolm F.; Allers, Thorsten

doi:10.1042/bst0370102

Cited by 50 publications

(72 citation statements)

References 41 publications

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“…HR is universally catalyzed by recombinases, i.e., RecA in bacteria, Rad51 in eukaryotes, and RadA in archaea (1,2). HR recombinases promote the exchange of homologous DNA strands, a prerequisite for which is the formation of a complex between ssDNA and the recombinase called the "presynaptic filament."…”

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confidence: 99%

Structure–function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation

Quevillon‐Chéruel

Campo

Mirouze

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

152

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Transformation promotes genome plasticity in bacteria via RecAdriven homologous recombination. In the Gram-positive human pathogen Streptococcus pneumoniae, the transformasome a multiprotein complex, internalizes, protects, and processes transforming DNA to generate chromosomal recombinants. Double-stranded DNA is internalized as single strands, onto which the transformation-dedicated DNA processing protein A (DprA) ensures the loading of RecA to form presynaptic filaments. We report that the structure of DprA consists of the association of a sterile alpha motif domain and a Rossmann fold and that DprA forms tail-totail dimers. The isolation of DprA self-interaction mutants revealed that dimerization is crucial for the formation of nucleocomplexes in vitro and for genetic transformation. Residues important for DprARecA interaction also were identified and mutated, establishing this interaction as equally important for transformation. Positioning of key interaction residues on the DprA structure revealed an overlap of DprA-DprA and DprA-RecA interaction surfaces. We propose a model in which RecA interaction promotes rearrangement or disruption of the DprA dimer, enabling the subsequent nucleation of RecA and its polymerization onto ssDNA.bacterial transformation | genetic exchange | recombinase loader | recombination mediator protein | horizontal gene transfer

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mentioning

confidence: 99%

Structure–function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation

Quevillon‐Chéruel

Campo

Mirouze

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

152

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“…Euryarchaeal RadB and crenarchaeal stRadC2 are known to inhibit RadA recombination activity, which has enriched our knowledge on crenarchaeal DNA recombination. In addition, stRadC2 interacts with Hjc and facilitates the resolution of Holliday DNA junctions, which is more similar to its eukaryotic equivalents [3][4][5][6] than to its euryarchaeal ones [9,10]. At the late stages of DNA recombination, the cell ends DNA repair and starts normal metabolism.…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, sequence alignment showed that some of these proteins, for instance, SSO2452 and SSO1861 in S. solfataricus, and ST0579 and ST1830 in S. tokodaii were more similar to the KaiC-like proteins than to any known RadA/Rad51 paralog found throughout archaea and eukarya. Therefore, these proteins were named RadC by Haldenby [9]. However, the real roles of RadC proteins in archaea remain unclear.…”

mentioning

confidence: 99%

“…In addition, RadB can interact with RadA directly and repress the recombination activity of RadA [11]. In Haloferax volcanii, deletion of radB results in growth retardation, increased sensitivity to UV light and recombination defects, suggesting a role of RadB as a recombination mediator [9]. The hyperthermophilic crenarchaea, another branch of archaea, has several RadA homologs, such as SSO2452, SSO1861 and SSO0777 in Sulfolobus solfataricus, and ST0579, ST0838, ST1830 and ST2522 in S. tokodaii [12][13][14].…”

mentioning

confidence: 99%

“…Accordingly, archaea possess recombinase RadA paralogs [9]. In euryarchaea, Pyrococcus furious has one RadA paralog, named RadB.…”

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confidence: 99%

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Sulfolobus tokodaii RadA paralog, stRadC2, is involved in DNA recombination via interaction with RadA and Hjc

Wang

Sheng

Han

et al. 2012

Sci. China Life Sci.

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Rad51/RadA paralogs found in eukaryotes and euryarchaea play important roles during recombination and repair, and mutations in one of the human Rad51 paralogs, Rad51C, are associated with breast and ovarian cancers. The hyperthermophilic crenarchaeon Sulfolobus tokodaii encodes four putative RadA paralogs and studies on these proteins may assist in understanding the functions of human Rad51 paralogs. Here, we report the biochemical characterization of stRadC2, a S. tokodaii RadA paralog. Pull-down assays revealed that the protein was able to interact with the recombinase, RadA, and the Holliday junction endonuclease, Hjc. stRadC2 inhibited the strand exchange activity of RadA and facilitated Hjc-mediated Holliday junction DNA cleavage in vitro. RT-PCR analysis revealed that stRadC2 transcription was immediately reduced after UV irradiation, but was restored to normal levels at the late stages of DNA repair. Our results suggest that stRadC2 may act as an anti-recombination factor in DNA recombinational repair in S. tokodaii.

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Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly

Meshcheryakov

Wolf

2016

Protein Science

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Archaeal flagella are unique structures that share functional similarity with bacterial flagella, but are structurally related to bacterial type IV pili. The flagellar accessory protein FlaH is one of the conserved components of the archaeal motility system. However, its function is not clearly understood. Here, we present the 2.2 Å resolution crystal structure of FlaH from the hyperthermophilic archaeon, Methanocaldococcus jannaschii. The protein has a characteristic RecA-like fold, which has been found previously both in archaea and bacteria. We show that FlaH binds to immobilized ATP-however, it lacks ATPase activity. Surface plasmon resonance analysis demonstrates that ATP affects the interaction between FlaH and the archaeal motor protein FlaI. In the presence of ATP, the FlaH-FlaI interaction becomes significantly weaker. A database search revealed similarity between FlaH and several DNA-binding proteins of the RecA superfamily. The closest structural homologs of FlaH are KaiC-like proteins, which are archaeal homologs of the circadian clock protein KaiC from cyanobacteria. We propose that one of the functions of FlaH may be the regulation of archaeal motor complex assembly.

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RecA family proteins in archaea: RadA and its cousins

Cited by 50 publications

References 41 publications

Structure–function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation

Structure–function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation

Sulfolobus tokodaii RadA paralog, stRadC2, is involved in DNA recombination via interaction with RadA and Hjc

Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly

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