Proteomics

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

ABSTRACT: Budding yeast Tsr1 is an essential ribosome biogenesis factor that is required for cytoplasmic steps in 40S subunit maturation. S. cerevisiae Tsr1 was expressed as an N-terminal GST fusion protein in E. coli. A mutant Tsr1ΔNΔloop was generated in which residues 410 to 476 of Tsr1 were replaced with a short glycine and serine rich sequence; in addition, the N-ternimal 45 amino acid residues were replaced by five amino acid residues “GPDSD”. Tsr1ΔNΔloop allowed for generating native crystals that diffracted to 3.6 Å. Here we characterize both wild type Tsr1 and Tsr1ΔNΔloop using cross-linking/mass spectrometry.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Zhuo Chen  

LAB HEAD: Juri Rappsilber

PROVIDER: PXD004074 | Pride | 2017-02-08

REPOSITORIES: pride

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Dataset's files

Source:
Action DRS
Rappsilber_Cook_CLMS_Tsr1_Mutant.raw Raw
Rappsilber_Cook_CLMS_Tsr1_Peaklist.zip Other
Rappsilber_Cook_CLMS_Tsr1_SearchResult.csv Csv
Rappsilber_Cook_CLMS_Tsr1_WildType1.raw Raw
Rappsilber_Cook_CLMS_Tsr1_WildType2.raw Raw
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Publications

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

McCaughan Urszula M UM   Jayachandran Uma U   Shchepachev Vadim V   Chen Zhuo Angel ZA   Rappsilber Juri J   Tollervey David D   Cook Atlanta G AG  

Nature communications 20160602

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 T  ...[more]

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