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JustinA posted in Plaques appear on spot test, don't appear in titer
Viknesh Sivanathan posted in Plaques appear on spot test, don't appear in titer
JustinA posted in Plaques appear on spot test, don't appear in titer
Viknesh Sivanathan posted in Plaques appear on spot test, don't appear in titer
RyanWheeler posted in Plaques appear on spot test, don't appear in titer
DNA ds break repair Mre11
Link to this post | posted 11 Aug, 2017 13:55 | |
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In the annotation of Biglebops_31 (27784-28920) we found multiple hits to endonucleases (Hammy_34, Vendetta_66, Splinter_66) and to exonucleases LindNT_35, Marcoliusprime_34), all with e-values of 0. HHPRED also had several hits to endo- and exo-nucleases as well as hits to MRE11 which has both activities and is a DNA double-strand break repair protein (99.5% probability, 60-70% coverage and e-values 10^-12 to 10^-14) that pairs with RAD50, an ATPase. We have no accepted annotation that would best fit this situation. Could we add a "DNA double strand break repair, Mre11-like protein" annotation function to our accepted list? I have included below, an associated paper abstract for the top hit 1ii7_A that explains the relationship of Mre11 and Rad50. Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase. Hopfner, K.P., Karcher, A., Craig, L., Woo, T.T., Carney, J.P., Tainer, J.A. (2001) Cell(Cambridge,Mass.) 105: 473-485 PubMed: 11371344 Search on PubMed Primary Citation of Related Structures: 1II7 1II8 PubMed Abstract: To clarify functions of the Mre11/Rad50 (MR) complex in DNA double-strand break repair, we report Pyrococcus furiosus Mre11 crystal structures, revealing a protein phosphatase-like, dimanganese binding domain capped by a unique domain controlling active site access. These structures unify Mre11's multiple nuclease activities in a single endo/exonuclease mechanism and reveal eukaryotic macromolecular interaction sites by mapping human and yeast Mre11 mutations. Furthermore, the structure of the P. furiosus Rad50 ABC-ATPase with its adjacent coiled-coil defines a compact Mre11/Rad50-ATPase complex and suggests that Rad50-ATP-driven conformational switching directly controls the Mre11 exonuclease. Electron microscopy, small angle X-ray scattering, and ultracentrifugation data of human and P. furiosus MR reveal a dual functional complex consisting of a (Mre11)2/(Rad50)2 heterotetrameric DNA processing head and a double coiled-coil linker. |
Link to this post | posted 14 Aug, 2017 13:50 | |
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Hi Claire, Welkin had given the ok to add MRE11 double-strand break endo/exonuclease. See the post below: https://seaphages.org/forums/topic/4346/?page=1#post-5533 Best, Jackie |