Pre-40S ribosome biogenesis factor Tsr1 is an inactive structural mimic of translational GTPases

Urszula M. McCaughan, Uma Jayachandran, Vadim Shchepachev, Zhuo Angel Chen, Juri Rappsilber, David Tollervey and Atlanta G. Cook ()
Additional contact information
Urszula M. McCaughan: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Uma Jayachandran: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Vadim Shchepachev: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Zhuo Angel Chen: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Juri Rappsilber: Wellcome Trust Centre for Cell Biology, University of Edinburgh
David Tollervey: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Atlanta G. Cook: Wellcome Trust Centre for Cell Biology, University of Edinburgh

Nature Communications, 2016, vol. 7, issue 1, 1-8

Abstract: Abstract Budding yeast Tsr1 is a ribosome biogenesis factor with sequence similarity to GTPases, which is essential for cytoplasmic steps in 40S subunit maturation. Here we present the crystal structure of Tsr1 at 3.6 Å. Tsr1 has a similar domain architecture to translational GTPases such as EF-Tu and the selenocysteine incorporation factor SelB. However, active site residues required for GTP binding and hydrolysis are absent, explaining the lack of enzymatic activity in previous analyses. Modelling of Tsr1 into cryo-electron microscopy maps of pre-40S particles shows that a highly acidic surface of Tsr1 is presented on the outside of pre-40S particles, potentially preventing premature binding to 60S subunits. Late pre-40S maturation also requires the GTPase eIF5B and the ATPase Rio1. The location of Tsr1 is predicted to block binding by both factors, strongly indicating that removal of Tsr1 is an essential step during cytoplasmic maturation of 40S ribosomal subunits.

Date: 2016
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms11789 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11789

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms11789

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().