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RRM domain of human RBM7: purification, crystallization and structure determination

DOI: 10.1107/S2053230X16006129 DOI Help

Authors: Nicholas Sofos (Aarhus University) , Mikael B. L. Winkler (Aarhus University) , Ditlev E. Brodersen (Aarhus University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 72 , PAGES 397 - 402

State: Published (Approved)
Published: May 2016
Diamond Proposal Number(s): 9317

Abstract: RNA decay is an important process that is essential for controlling the abundance, quality and maturation of transcripts. In eukaryotes, RNA decay in the 3′–5′ direction is carried out by the exosome, an RNA-degradation machine that is conserved from yeast to humans. A range of cofactors stimulate the enzymatic activity of the exosome and serve as adapters for the many RNA substrates. In human cells, the exosome associates with the heterotrimeric nuclear exosome targeting (NEXT) complex consisting of the DExH-box helicase hMTR4, the zinc-finger protein hZCCHC8 and the RRM-type protein hRBM7. Here, the 2.5 Å resolution crystal structure of the RRM domain of human RBM7 is reported. Molecular replacement using a previously determined solution structure of RBM7 was unsuccessful. Instead, RBM8 and CBP20 RRM-domain crystal structures were used to successfully determine the RBM7 structure by molecular replacement. The structure reveals a ring-shaped pentameric assembly, which is most likely a consequence of crystal packing.

Journal Keywords: RNA degradation; human; NEXT complex; RRM domain; X-ray crystallography

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

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