Structure of the Yeast DEAD Box Protein Mss116p Reveals Two Wedges that Crimp RNA

Journal Article · Tue Jan 12 04:00:00 EST 2010 · Mol. Cell

DOI:https://doi.org/10.1016/j.molcel.2009.07.032· OSTI ID:1006057

Del Campo, Mark; Lambowitz, Alan M

The yeast DEAD box protein Mss116p is a general RNA chaperone that functions in mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Here we determined high-resolution X-ray crystal structures of Mss116p complexed with an RNA oligonucleotide and ATP analogs AMP-PNP, ADP-BeF{sub 3}, or ADP-AlF{sub 4}{sup -}. The structures show the entire helicase core acting together with a functionally important C-terminal extension. In all structures, the helicase core is in a closed conformation with a wedge {alpha} helix bending RNA 3' of the central bound nucleotides, as in previous DEAD box protein structures. Notably, Mss116p's C-terminal extension also bends RNA 5' of the central nucleotides, resulting in RNA crimping. Despite reported functional differences, we observe few structural changes in ternary complexes with different ATP analogs. The structures constrain models of DEAD box protein function and reveal a strand separation mechanism in which a protein uses two wedges to act as a molecular crimper.

• Research Organization: Argonne National Laboratory (ANL)
• Sponsoring Organization: USDOE
• OSTI ID: 1006057
• Journal Information: Mol. Cell, Journal Name: Mol. Cell Journal Issue: (5) ; 09, 2009 Vol. 35; ISSN 1097-2765
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
BENDING
CRYSTAL STRUCTURE
FUNCTIONALS
INTRONS
NUCLEOTIDES
OLIGONUCLEOTIDES
PROCESSING
PROTEIN STRUCTURE
PROTEINS
RNA
SPLICING
YEASTS