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User:Sdorlean

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CACAO Spring 2018

My Annotations

StatusPageDate/TimeGO Term (Aspect)ReferenceEvidenceNotesLinks
updatedbyinstructorCAEEL:RFS12018-04-11 10:18:48 CDTGO:0000730 DNA recombinase assembly (P)PMID:27867009ECO:0000316 genetic interaction evidence used in manual assertion

Figure 1 depicts the cessation of the dissociation of RAD-51 from ssDNA due to the presence of protein RFS-1/RIP-1. Figure 1, Part H [(i), (ii)] shows the known mechanism of RAD-51 by demonstrating that it’s presence prohibits the binding of ScRPA-eGFP-ssDNA. The incapability of RAD-51 to be expressed due to the lack of ATP is found in Figure 1, Part H (ii). Figure 1 ultimately illustrates that in the precence of the protein RFS-1/RIP-1 and ATP; RAD-51 along with the protein RFS-1/RIP-1 is present but the ScRPA-eGFP-ssDNA are not [(Figure 1, Part H (iii)]. The same events occur when the protein RFS-1/RIP-1 is present but not ATP [(Figure 1, Part H (iv)].

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updatedbyinstructorCAEEL:RFS12018-04-13 08:05:13 CDTGO:0000730 DNA recombinase assembly (P)PMID:26186187ECO:0000316 genetic interaction evidence used in manual assertion

Figure 2 provides the biochemical properties of the RFS-1/RIP-1 complex. The western blot in part A of this figure confirms the precence of the two proteins (RFS-1/RIP-1) after co-purifying the recombinant proteins from budding yeast cells. The Electrophoretic mobility shift assays (EMSA) shown in part B of the figure reveals that the RFS-1/RIP-1 complex binds in a nucleotide independent manner weakly to ssDNA but not dsDNA. Bands are observed only for ssDNA. The RFS-1/RIP-1 complex can also stimulate D loop formations with RAD51 (C) and the fact that ATP is required to do so (D).

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