3P27

Crystal structure of S. cerevisiae Hbs1 protein (GDP-bound form), a translational GTPase involved in RNA quality control pathways and interacting with Dom34/Pelota

Summary for 3P27

• Entry DOI: 10.2210/pdb3p27/pdb
• Related: 3P26
• Descriptor: Elongation factor 1 alpha-like protein, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: gdp/gtp binding domain, beta-barrel, translational gtpase, structural genomics, paris-sud yeast structural genomics, ysg, signaling protein
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• Cellular location: Cytoplasm: P32769
• Total number of polymer chains: 2
• Total formula weight: 110573.75

Authors

van den Elzen, A.,Henri, J.,Lazar, N.,Gas, M.E.,Durand, D.,Lacroute, F.,Nicaise, M.,van Tilbeurgh, H.,Sraphin, B.,Graille, M.,Paris-Sud Yeast Structural Genomics (YSG) (deposition date: 2010-10-01, release date: 2010-11-17, Last modification date: 2024-10-30)

Primary citation

van den Elzen, A.M.,Henri, J.,Lazar, N.,Gas, M.E.,Durand, D.,Lacroute, F.,Nicaise, M.,van Tilbeurgh, H.,Seraphin, B.,Graille, M.
Dissection of Dom34-Hbs1 reveals independent functions in two RNA quality control pathways.
Nat.Struct.Mol.Biol., 17:1446-1452, 2010

PubMed Abstract: Eukaryotic cells have several quality control pathways that rely on translation to detect and degrade defective RNAs. Dom34 and Hbs1 are two proteins that are related to translation termination factors and are involved in no-go decay (NGD) and nonfunctional 18S ribosomal RNA (rRNA) decay (18S NRD) pathways that eliminate RNAs that cause strong ribosomal stalls. Here we present the structure of Hbs1 with and without GDP and a low-resolution model of the Dom34-Hbs1 complex. This complex mimics complexes of the elongation factor and transfer RNA or of the translation termination factors eRF1 and eRF3, supporting the idea that it binds to the ribosomal A-site. We show that nucleotide binding by Hbs1 is essential for NGD and 18S NRD. Mutations in Hbs1 that disrupted the interaction between Dom34 and Hbs1 strongly impaired NGD but had almost no effect on 18S NRD. Hence, NGD and 18S NRD could be genetically uncoupled, suggesting that mRNA and rRNA in a stalled translation complex may not always be degraded simultaneously.

PubMed: 21102444
DOI: 10.1038/nsmb.1963

Experimental method

X-RAY DIFFRACTION (2.95 Å)