Journal
NATURE COMMUNICATIONS
Volume 10, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-10678-z
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Funding
- METI platform, CBI, Toulouse, France
- CM01 beamline, ESRF, Grenoble, France
- Biophysical and Structural Chemistry platform (BPCS) at IECB, CNRS UMS3033, Inserm US001, Bordeaux University, France
- CALMIP [2018-[P1406]]
- Austrian Science Fund (FWF) [P27996-B21, P28874-B21]
- Swiss National Science Foundation (SNSF) [31003A_156764, 31003A_175547]
- Department of Biochemistry III, House of the Ribosome
- DFG collaborative research center [SFB960-AP1]
- DFG grant [409198929 - FE 1622/2-1]
- German Research Foundation (DFG)
- grant RIBOMAN from the French National Research Agency (ANR)
- Swiss National Science Foundation (SNF) [31003A_175547, 31003A_156764] Funding Source: Swiss National Science Foundation (SNF)
- Austrian Science Fund (FWF) [P28874] Funding Source: Austrian Science Fund (FWF)
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Eukaryotic ribosomes are synthesized in a hierarchical process driven by a plethora of assembly factors, but how maturation events at physically distant sites on pre-ribosomes are coordinated is poorly understood. Using functional analyses and cryo-EM, we show that ribosomal protein Rps20 orchestrates communication between two multi-step maturation events across the pre-40S subunit. Our study reveals that during pre-40S maturation, formation of essential contacts between Rps20 and Rps3 permits assembly factor Ltv1 to recruit the Hrr25 kinase, thereby promoting Ltv1 phosphorylation. In parallel, a deeply buried Rps20 loop reaches to the opposite pre-40S side, where it stimulates Rio2 ATPase activity. Both cascades converge to the final maturation steps releasing Rio2 and phosphorylated Ltv1. We propose that conformational proofreading exerted via Rps20 constitutes a checkpoint permitting assembly factor release and progression of pre-40S maturation only after completion of all earlier maturation steps.
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