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PMID:12627222

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Citation

Ohi, MD, Vander Kooi, CW, Rosenberg, JA, Chazin, WJ and Gould, KL (2003) Structural insights into the U-box, a domain associated with multi-ubiquitination. Nat. Struct. Biol. 10:250-5

Abstract

The structure of the U-box in the essential Saccharomyces cerevisiae pre-mRNA splicing factor Prp19p has been determined by NMR. The conserved zinc-binding sites supporting the cross-brace arrangement in RING-finger domains are replaced by hydrogen-bonding networks in the U-box. These hydrogen-bonding networks are necessary for the structural stabilization and activity of the U-box. A conservative Val-->Ile point mutation in the Prp19p U-box domain leads to pre-mRNA splicing defects in vivo. NMR analysis of this mutant shows that the substitution disrupts structural integrity of the U-box domain. Furthermore, comparison of the Prp19p U-box domain with known RING-E2 complex structures demonstrates that both U-box and RING-fingers contain a conserved interaction surface. Mutagenesis of residues at this interface, while not perturbing the structure of the U-box, abrogates Prp19p function in vivo. These comparative structural and functional analyses imply that the U-box and its associated ubiquitin ligase activity are critical for Prp19p function in vivo.

Links

PubMed Online version:10.1038/nsb906

Keywords

Amino Acid Sequence; Drug Stability; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Tertiary; RNA Splicing; Saccharomyces cerevisiae Proteins/chemistry; Saccharomyces cerevisiae Proteins/genetics; Sequence Homology, Amino Acid; Spliceosomes; Ubiquitin/chemistry

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

YEAST:PRP19

enables

GO:0004842: ubiquitin-protein transferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

YEAST:PRP19

enables

GO:0004842: ubiquitin-protein transferase activity

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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