5M1X

Crystal structure of S. cerevisiae Rfa1 N-OB domain mutant (K45E)

Summary for 5M1X

• Entry DOI: 10.2210/pdb5m1x/pdb
• Descriptor: Replication factor A protein 1 (2 entities in total)
• Functional Keywords: ob fold, replication
• Biological source: Saccharomyces cerevisiae S288c (Baker's yeast)
• Cellular location: Nucleus: P22336
• Total number of polymer chains: 4
• Total formula weight: 62467.02

Authors

Seeber, A.,Hegnauer, A.M.,Hustedt, N.,Deshpande, I.,Poli, J.,Eglinger, J.,Pasero, P.,Gut, H.,Shinohara, M.,Hopfner, K.P.,Shimada, K.,Gasser, S.M. (deposition date: 2016-10-11, release date: 2016-12-07, Last modification date: 2024-10-23)

Primary citation

Seeber, A.,Hegnauer, A.M.,Hustedt, N.,Deshpande, I.,Poli, J.,Eglinger, J.,Pasero, P.,Gut, H.,Shinohara, M.,Hopfner, K.P.,Shimada, K.,Gasser, S.M.
RPA Mediates Recruitment of MRX to Forks and Double-Strand Breaks to Hold Sister Chromatids Together.
Mol. Cell, 64:951-966, 2016

PubMed Abstract: The Mre11-Rad50-Xrs2 (MRX) complex is related to SMC complexes that form rings capable of holding two distinct DNA strands together. MRX functions at stalled replication forks and double-strand breaks (DSBs). A mutation in the N-terminal OB fold of the 70 kDa subunit of yeast replication protein A, rfa1-t11, abrogates MRX recruitment to both types of DNA damage. The rfa1 mutation is functionally epistatic with loss of any of the MRX subunits for survival of replication fork stress or DSB recovery, although it does not compromise end-resection. High-resolution imaging shows that either the rfa1-t11 or the rad50Δ mutation lets stalled replication forks collapse and allows the separation not only of opposing ends but of sister chromatids at breaks. Given that cohesin loss does not provoke visible sister separation as long as the RPA-MRX contacts are intact, we conclude that MRX also serves as a structural linchpin holding sister chromatids together at breaks.

PubMed: 27889450
DOI: 10.1016/j.molcel.2016.10.032

Experimental method

X-RAY DIFFRACTION (1.8 Å)