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Protein Sci. 2018 Dec;27(12):2094-2100. doi: 10.1002/pro.3515. Epub 2018 Nov 5.

The budding-yeast RWD protein Csm1 scaffolds diverse protein complexes through a conserved structural mechanism.

Author information

1
Ludwig Institute for Cancer Research, San Diego Branch, La Jolla, California, 92093.
2
Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, California, 92093.
3
Department of Chemistry, University of California, San Diego, La Jolla, California, 92093.

Abstract

RWD domains mediate protein-protein interactions in a variety of pathways in eukaryotes. In budding yeast, the RWD domain protein Csm1 is particularly versatile, assembling key complexes in the nucleolus and at meiotic kinetochores through multiple protein interaction surfaces. Here, we reveal a third functional context for Csm1 by identifying a new Csm1-interacting protein, Dse3. We show that Dse3 interacts with Csm1 in a structurally equivalent manner to its known binding partners Mam1 and Ulp2, despite these three proteins' lack of overall sequence homology. We theorize that the unique "clamp" structure of Csm1 and the loose sequence requirements for Csm1 binding have led to its incorporation into at least three different structural/signaling pathways in budding yeast.

KEYWORDS:

RWD domain; S. cerevisiae; X-ray crystallography; monopolin complex; protein-protein interactions

PMID:
30252178
PMCID:
PMC6237700
[Available on 2019-12-01]
DOI:
10.1002/pro.3515

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