Data on Rad51 amino acid sequences from higher and lower eukaryotic model organisms and parasites

Kelso, Andrew A.; Goodson, Steven D.; Temesvari, Lesly A.; Sehorn, Michael G.

doi:10.1016/j.dib.2016.12.002

Cited by 5 publications

(9 citation statements)

References 8 publications

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“…Intriguingly we found that many of the biochemical properties of eh Rad51 are similar to human RAD51, which is in agreement with the high degree of sequence conservation between the eh Rad51 and human RAD51 (66%; Fig. 2 in [42]). For example, in our study, we confirmed that eh Rad51 binds ssDNA and dsDNA [29], and our results demonstrate that eh Rad51 preferentially bound ssDNA over dsDNA similar to human RAD51 [43].…”

Section: Discussionsupporting

confidence: 84%

“…1 in [42]) known to be important for binding and hydrolysis of ATP. To determine if eh Rad51 possessed the ability to hydrolyze ATP, purified eh Rad51 was incubated with saturating amounts of [ 32 P-γ]-ATP.…”

Section: Resultsmentioning

confidence: 99%

“…This is likely due to the high degree of homology between the human and murine RAD51 (99% identity) and DMC1 (97% identity) recombinases (Fig. 2 in [42]). E. histolytica has the HOP2 and MND1 genes and their expression is upregulated during encystation in E. histolytica at the same time as eh Rad51 and eh Dmc1 [33].…”

Section: Resultsmentioning

confidence: 99%

“…In addition to these studies, Ploquin et al (2007) showed mHop2-Mnd1 interacted with Schizosaccharomyces pombe Rad51 ( Sp Rad51) [19] despite lower sequence identity (74%) between Sp Rad51 and murine Rad51 (Fig. 2 in [42]). The ability of mHop2-Mnd1 to interact with human RAD51, human DMC1, Sp Rad51, and eh Dmc1 [17,19,37,40,60] combined with the sequence identity of eh Rad51 with murine RAD51 (65% identity) that is close to that of Sp Rad51 and murine RAD51 (74% identity) (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The ability of mHop2-Mnd1 to interact with human RAD51, human DMC1, Sp Rad51, and eh Dmc1 [17,19,37,40,60] combined with the sequence identity of eh Rad51 with murine RAD51 (65% identity) that is close to that of Sp Rad51 and murine RAD51 (74% identity) (Fig. 2 in [42]), led us to reason that mHop2-Mnd1 may interact with eh Rad51 thereby potentially enhancing its recombination activities. We first determined if mHop2-Mnd1 interacted with eh Rad51 by performing an affinity pull-down assay using either bovine serum albumin (BSA) or purified mHop2-Mnd1 immobilized on Affi-gel matrix [37].…”

Section: Resultsmentioning

confidence: 99%

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Characterization of the recombination activities of the Entamoeba histolytica Rad51 recombinase

Kelso

Goodson

Chavan

et al. 2016

Molecular and Biochemical Parasitology

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The protozoan parasite responsible for human amoebiasis is Entamoeba histolytica. An important facet of the life cycle of E. histolytica involves the conversion of the mature trophozoite to a cyst. This transition is thought to involve homologous recombination (HR), which is dependent upon the Rad51 recombinase. Here, a biochemical characterization of highly purified ehRad51 protein is presented. The ehRad51 protein preferentially binds ssDNA, forms a presynaptic filament and possesses ATP hydrolysis activity that is stimulated by the presence of DNA. Evidence is provided that ehRad51 catalyzes robust DNA strand exchange over at least 5.4 kilobase pairs. Although the homologous DNA pairing activity of ehRad51 is weak, it is strongly enhanced by the presence of two HR accessory cofactors, calcium and Hop2-Mnd1. The biochemical system described herein was used to demonstrate the potential for targeting ehRad51 with two small molecule inhibitors of human RAD51. We show that 4,4′-diisothiocyanostilbene-2,2′-disulfonic acid (DIDS) inhibited ehRad51 by interfering with DNA binding and attenuated encystation in Entamoeba invadens, while B02 had no effect on ehRad51 strand exchange activity. These results provide insight into the underlying mechanism of homology-directed DNA repair in E. histolytica.

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Section: Discussionsupporting

confidence: 84%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Characterization of the recombination activities of the Entamoeba histolytica Rad51 recombinase

Kelso

Goodson

Chavan

et al. 2016

Molecular and Biochemical Parasitology

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spn-A/rad51 mutant exhibits enhanced genomic damage, cell death and low temperature sensitivity in somatic tissues

et al. 2020

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dmrad51/spnAmutant exhibit defects during somatic stages of developmental and show enhanced genomic damage, cell death and low temperature sensitivity

Khan

Muliyil

Ayyub

et al. 2017

Preprint

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Homologous Recombination (HR) is one of the key pathways to repair Double Strand Breaks (DSBs). Rad51 serves an important function of catalysing strand exchange between two homologous chromosomes in the HR pathway. In higher organisms, Rad51 function is indispensable with its absence leading to early embryonic lethality, thus precluding any mechanistic probing of the system. In contrast, absence of Drosophila rad51 (Dmrad51/spnA) has been associated with defects in female germline causing ventralization of the egg, without any reported detrimental consequences to Drosophila somatic tissues. In this study, we have performed a systematic analysis of somatic development of dmrad51 null mutant flies by using genetic complementation between multiple dmrad51 alleles. Our current study, for the first time, uncovers the requirement of Dmrad51 in somatic tissue maintenance at both larval and pupal stages. Also, we show that dmrad51 mutant exhibit patterning defects not peer-reviewed) is the author/funder. All rights reserved. No reuse allowed without permission.The copyright holder for this preprint (which was . http://dx.doi.org/10.1101/180737 doi: bioRxiv preprint first posted online Aug. 25, 2017; 2 in abdominal cuticle in the stripes and bristles, while there appears to be only subtle defects in the adult wing and eye. Interestingly, dmrad51 null mutant and other alleles show discernible phenotype of low temperature sensitivity, suggesting a role for Dmrad51 in temperature sensitive cellular processes, which thus presents an elegant system for probing temperature sensitive cellular/tissue responses that ensue when a mutation leads to the loss of protein expression (null mutant) rather than its altered protein structure. In summary, our study describes the role of Dmrad51 during somatic stages of development and provides a viable model system to study Rad51 function in a cellular process.

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Data on Rad51 amino acid sequences from higher and lower eukaryotic model organisms and parasites

Cited by 5 publications

References 8 publications

Characterization of the recombination activities of the Entamoeba histolytica Rad51 recombinase

Characterization of the recombination activities of the Entamoeba histolytica Rad51 recombinase

spn-A/rad51 mutant exhibits enhanced genomic damage, cell death and low temperature sensitivity in somatic tissues

dmrad51/spnAmutant exhibit defects during somatic stages of developmental and show enhanced genomic damage, cell death and low temperature sensitivity

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