Structural basis for the function of DEAH helicases

TY - JOUR

T1 - Structural basis for the function of DEAH helicases

AU - He, Yangzi

AU - Andersen, Gregers Rom

AU - Nielsen, Klaus Hvid

N1 - Paper id:: 10.1038/embor.2010.11

PY - 2010/2/19

Y1 - 2010/2/19

N2 - 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 β‐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.

AB - 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 β‐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.

U2 - 10.1038/embor.2010.11

DO - 10.1038/embor.2010.11

M3 - Journal article

C2 - 20168331

SN - 1469-221X

VL - 11

SP - 180

EP - 186

JO - E M B O Reports

JF - E M B O Reports

IS - 3

ER -