Interdependent action of KH domain proteins Krr1 and Dim2 drive the 40S platform assembly

Miriam Sturm; Jingdong Cheng; Jochen Baßler; Roland Beckmann; Ed Hurt

doi:10.1038/s41467-017-02199-4

Nature Communications (Dec 2017)

Interdependent action of KH domain proteins Krr1 and Dim2 drive the 40S platform assembly

Miriam Sturm,
Jingdong Cheng,
Jochen Baßler,
Roland Beckmann,
Ed Hurt

Affiliations

Miriam Sturm: Biochemistry Centre, University of Heidelberg
Jingdong Cheng: Department of Biochemistry, Gene Center, Center for integrated Protein Science - Munich (CiPS-M), Ludwig-Maximillian University
Jochen Baßler: Biochemistry Centre, University of Heidelberg
Roland Beckmann: Department of Biochemistry, Gene Center, Center for integrated Protein Science - Munich (CiPS-M), Ludwig-Maximillian University
Ed Hurt: Biochemistry Centre, University of Heidelberg

DOI: https://doi.org/10.1038/s41467-017-02199-4
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 13

Abstract

Read online

The biogenesis of eukaryotic ribosomes involves the coordinated interplay of a large number of assembly factors. Here, the authors detail how the conserved KH domain-containing assembly factors Dim2 and Krr1 function in ordering key events during ribosome maturation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal