Cryo-EM structure of the Smc5/6 holo-complex

The Smc5/6 complex plays an essential role in the resolution of recombination intermediates formed during mitosis or meiosis, or as a result of the cellular response to replication stress. It also functions as a restriction factor preventing viral integration. Here, we report the cryo-EM structure o...

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Vydáno v:bioRxiv
Hlavní autoři: Hallett, Stephen T, Campbell, Isabella, Schellenberger, Pascale, Zhou, Lihong, Cronin, Nora B, Baxter, Jonathan, Etheridge, Thomas J, Murray, Johanne M, Oliver, Antony W
Médium: Paper
Jazyk:angličtina
Vydáno: Cold Spring Harbor Cold Spring Harbor Laboratory Press 26.11.2021
Cold Spring Harbor Laboratory
Vydání:1.2
Témata:
Biochemistry
Insect cells
Intermediates
Meiosis
Mitosis
Recombination
ISSN:2692-8205, 2692-8205
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Shrnutí:The Smc5/6 complex plays an essential role in the resolution of recombination intermediates formed during mitosis or meiosis, or as a result of the cellular response to replication stress. It also functions as a restriction factor preventing viral integration. Here, we report the cryo-EM structure of the six-subunit budding yeast Smc5/6 holo-complex, reconstituted from recombinant proteins expressed in insect cells --providing a full overview of the complex in its apo / non-liganded form, and revealing how the Nse1/3/4 subcomplex binds to the hetero-dimeric SMC protein core. In addition, we demonstrate that a region within the head domain of Smc5, equivalent to the "W-loop" of Smc4 or "F-loop" of Smc1, mediates an essential interaction with Nse1. Taken together, these data confirm a degree of functional equivalence between the structurally unrelated KITE and HAWK accessory subunits associated with SMC complexes. Competing Interest Statement The authors have declared no competing interest. Footnotes * An image duplication error was identified in supplementary figure 3a; for Smc5-Y isolate #2 and isolate #3, 24 hours / YP. This has been corrected in this revised version of the paper.
Bibliografie:SourceType-Working Papers-1
ObjectType-Working Paper/Pre-Print-1
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Competing Interest Statement: The authors have declared no competing interest.
ISSN:2692-8205
2692-8205
DOI:10.1101/2021.11.25.470006