Journal
NUCLEIC ACIDS RESEARCH
Volume 44, Issue 2, Pages 926-939Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkv1365
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Funding
- Deutsche Forschungsgemeinschaft (DFG) [HU363/10-5, HU363/12-1, SFB 63, GRK1188]
- DFG/Uni Heidelberg EcTop1
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The complicated process of eukaryotic ribosome biogenesis involves about 200 assembly factors that transiently associate with the nascent pre-ribosome in a spatiotemporally ordered way. During the early steps of 60S subunit formation, several proteins, collectively called A(3) cluster factors, participate in the removal of the internal transcribed spacer 1 (ITS1) from 27SA(3) pre-rRNA. Among these factors is the conserved hetero-trimeric Nop7-Erb1-Ytm1 complex (or human Pes1-Bop1-Wdr12), which is removed from the evolving pre-60S particle by the AAA ATPase Rea1 to allow progression in the pathway. Here, we clarify how Ytm1 and Erb1 interact, which has implications for the release mechanism of both factors from the pre-ribosome. Biochemical studies show that Ytm1 and Erb1 bind each other via their beta-propeller domains. The crystal structure of the Erb1-Ytm1 heterodimer determined at 2.67 angstrom resolution reveals an extended interaction surface between the propellers in a rarely observed binding mode. Structure-based mutations in the interface that impair the Erb1-Ytm1 interaction do not support growth, with specific defects in 60S subunit synthesis. Under these mutant conditions, it becomes clear that an intact Erb1-Ytm1 complex is required for 60S maturation and that loss of this stable interaction prevents ribosome production.
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