Structural basis for the function of DEAH helicases.
DEAH helicases participate in pre-messenger RNA splicing and ribosome biogenesis. The structure of yeast Prp43p-ADP reveals the homology of DEAH helicases to DNA helicases and the presence of an oligonucleotide-binding motif. A beta-hairpin from the second RecA domain is wedged between two carboxy-terminal domains and blocks access to the occluded RNA binding site formed by the RecA domains and a C-terminal domain. ATP binding and hydrolysis are likely to induce conformational changes in the hairpin that are important for RNA unwinding or ribonucleoprotein remodelling. The structure of Prp43p provides the framework for functional and genetic analysis of all DEAH helicases.
He
Yangzi
Y
Department of Molecular Biology, Aarhus University, Aarhus, Denmark.
Andersen
Gregers R
GR
Nielsen
Klaus H
KH
D000255:Adenosine Triphosphate / Q000737:chemistry*; D017398:Alternative Splicing; D001665:Binding Sites; D018360:Crystallography, X-Ray / Q000379:methods; D053487:DEAD-box RNA Helicases / Q000235:genetics*; D004265:DNA Helicases / Q000378:metabolism*; D008958:Models, Molecular; D008968:Molecular Conformation; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry; D012326:RNA Splicing; D012333:RNA, Messenger / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics*
D012333:RNA, Messenger; D029701:Saccharomyces cerevisiae Proteins; D012313:RNA; D000255:Adenosine Triphosphate; C109034:PRP43 protein, S cerevisiae; D004265:DNA Helicases; D053487:DEAD-box RNA Helicases