ArticleBMC structural biology2009
Conformational flexibility and molecular interactions of an archaeal homologue of the Shwachman-Bodian-Diamond syndrome protein.
Article in BMC structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 31 citations in OpenAlex.
- Quality control ensures fidelity in ribosome assembly and cellular health.The Journal of cell biology · 2023Review
- A Comparative Molecular Dynamics Study of Selected Point Mutations in the Shwachman-Bodian-Diamond Syndrome Protein SBDS.International journal of molecular sciences · 2022Article
- Normal Mode Analysis as a Routine Part of a Structural Investigation.Molecules (Basel, Switzerland) · 2019Review
- Proteins of the Nucleolus ofCells · 2019Review
- Interaction of the GTPase Elongation Factor Like-1 with the Shwachman-Diamond Syndrome Protein and Its Missense Mutations.International journal of molecular sciences · 2018Article
- Molecular basis of the human ribosomopathy Shwachman-Diamond syndrome.Advances in biological regulation · 2018Review
- Structural dynamics of the yeast Shwachman-Diamond syndrome protein (Sdo1) on the ribosome and its implication in the 60S subunit maturation.Protein & cell · 2016Article
- Mechanism of eIF6 release from the nascent 60S ribosomal subunit.Nature structural & molecular biology · 2015Article
- HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions.Nature structural & molecular biology · 2015Article
- Bypass of the pre-60S ribosomal quality control as a pathway to oncogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Eukaryotic rpL10 drives ribosomal rotation.Nucleic acids research · 2014Article
- Essential ribosome assembly factor Fap7 regulates a hierarchy of RNA-protein interactions during small ribosomal subunit biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Clinical and molecular pathophysiology of Shwachman-Diamond syndrome: an update.Hematology/oncology clinics of North America · 2013Review
- Integrity of the P-site is probed during maturation of the 60S ribosomal subunit.The Journal of cell biology · 2012Article
- Structural and functional analysis of the archaeal endonuclease Nob1.Nucleic acids research · 2012Article
- Non-Diamond Blackfan anemia disorders of ribosome function: Shwachman Diamond syndrome and 5q- syndrome.Seminars in hematology · 2011Review
- Clinical spectrum and molecular pathophysiology of Shwachman-Diamond syndrome.Current opinion in hematology · 2011Review
- Altered intracellular localization and mobility of SBDS protein upon mutation in Shwachman-Diamond syndrome.PloS one · 2011Article
- Pathophysiology and management of inherited bone marrow failure syndromes.Blood reviews · 2010Review
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
Abstract
backgroundDefects in the human Shwachman-Bodian-Diamond syndrome (SBDS) protein-coding gene lead to the autosomal recessive disorder characterised by bone marrow dysfunction, exocrine pancreatic insufficiency and skeletal abnormalities. This protein is highly conserved in eukaryotes and archaea but is not found in bacteria. Although genomic and biophysical studies have suggested involvement of this protein in RNA metabolism and in ribosome biogenesis, its interacting partners remain largely unknown.
resultsWe determined the crystal structure of the SBDS orthologue from Methanothermobacter thermautotrophicus (mthSBDS). This structure shows that SBDS proteins are highly flexible, with the N-terminal FYSH domain and the C-terminal ferredoxin-like domain capable of undergoing substantial rotational adjustments with respect to the central domain. Affinity chromatography identified several proteins from the large ribosomal subunit as possible interacting partners of mthSBDS. Moreover, SELEX (Systematic Evolution of Ligands by EXponential enrichment) experiments, combined with electrophoretic mobility shift assays (EMSA) suggest that mthSBDS does not interact with RNA molecules in a sequence specific manner.
conclusionIt is suggested that functional interactions of SBDS proteins with their partners could be facilitated by rotational adjustments of the N-terminal and the C-terminal domains with respect to the central domain. Examination of the SBDS protein structure and domain movements together with its possible interaction with large ribosomal subunit proteins suggest that these proteins could participate in ribosome function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.