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Cryo-EM structure of the essential ribosome assembly AAA-ATPase Rix7
- Source :
- Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019), Nature Communications
- Publication Year :
- 2019
- Publisher :
- Nature Portfolio, 2019.
-
Abstract
- Rix7 is an essential type II AAA-ATPase required for the formation of the large ribosomal subunit. Rix7 has been proposed to utilize the power of ATP hydrolysis to drive the removal of assembly factors from pre-60S particles, but the mechanism of release is unknown. Rix7’s mammalian homolog, NVL2 has been linked to cancer and mental illness disorders, highlighting the need to understand the molecular mechanisms of this essential machine. Here we report the cryo-EM reconstruction of the tandem AAA domains of Rix7 which form an asymmetric stacked homohexameric ring. We trapped Rix7 with a polypeptide in the central channel, revealing Rix7’s role as a molecular unfoldase. The structure establishes that type II AAA-ATPases lacking the aromatic-hydrophobic motif within the first AAA domain can engage a substrate throughout the entire central channel. The structure also reveals that Rix7 contains unique post-α7 insertions within both AAA domains important for Rix7 function.<br />Rix7 is a type II AAA-ATPase that is required for the assembly of the large ribosomal subunit. Here the authors present the 4.5 Å cryo-EM structure of the Rix7 homohexamer with a polypeptide fragment bound in its central channel and provide insights into the function of Rix7 as a molecular unfoldase.
- Subjects :
- Adenosine Triphosphatases
Ribosomal Proteins
0303 health sciences
Multidisciplinary
Saccharomyces cerevisiae Proteins
Science
Cryoelectron Microscopy
General Physics and Astronomy
Nuclear Proteins
General Chemistry
Saccharomyces cerevisiae
macromolecular substances
General Biochemistry, Genetics and Molecular Biology
Article
03 medical and health sciences
0302 clinical medicine
RNA, Ribosomal
ATPases Associated with Diverse Cellular Activities
lcsh:Q
lcsh:Science
030217 neurology & neurosurgery
030304 developmental biology
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 10
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Nature Communications
- Accession number :
- edsair.doi.dedup.....532fd714ccd385a007693f08e99c8883