|Journal of Biological Chemistry (2005) 280(19):19213-20|
|Midwest Center for Structural GenomicsNortheast Structural Genomics Consortium|
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A combination of structural, biochemical, and genetic studies in model organisms was used to infer a cellular role for the human protein (SBDS) responsible for Shwachman-Bodian-Diamond syndrome. ...
The crystal structure of the SBDS homologue in Archaeoglobus fulgidus, AF0491, revealed a three domain protein. The N-terminal domain, which harbors the majority of disease-linked mutations, has a novel three-dimensional fold. The central domain has the common winged helix-turn-helix motif, and the C-terminal domain shares structural homology with known RNA-binding domains. Proteomic analysis of the SBDS sequence homologue in Saccharomyces cerevisiae, YLR022C, revealed an association with over 20 proteins involved in ribosome biosynthesis. NMR structural genomics revealed another yeast protein, YHR087W, to be a structural homologue of the AF0491 N-terminal domain. Sequence analysis confirmed them as distant sequence homologues, therefore related by divergent evolution. Synthetic genetic array analysis of YHR087W revealed genetic interactions with proteins involved in RNA and rRNA processing including Mdm20/Nat3, Nsr1, and Npl3. Our observations, taken together with previous reports, support the conclusion that SBDS and its homologues play a role in RNA metabolism.
|metabolism chemistry methods physiology |
|Crystallography, X-Ray Protein Structure, Tertiary Amino Acid Motifs Amino Acid Sequence Molecular Sequence Data Protein Binding Protein Structure, Secondary Proteins RNA-Binding Proteins Proteomics Protein Conformation Protein Folding Static Electricity Sequence Homology, Amino Acid RNA Phylogeny Genomics Saccharomyces cerevisiae Proteins Magnetic Resonance Spectroscopy Saccharomyces cerevisiae Nuclear Proteins Archaeoglobus fulgidus Acetyltransferases RNA, Ribosomal |
|80 (Last update: 01/19/2019 1:29:06pm)|
|J Biol Chem. 2005 May 13;280(19):19213-20. Epub 2005 Feb 8.|