Factor-dependent processivity in human eIF4A DEAD-box helicase

Author:

García-García Cuauhtémoc1,Frieda Kirsten L.2,Feoktistova Kateryna3,Fraser Christopher S.3,Block Steven M.14

Affiliation:

1. Department of Biology, Stanford University, Stanford, CA 94305, USA.

2. Biophysics Program, Stanford University, Stanford, CA 94305, USA.

3. Department of Molecular and Cellular Biology, University of California at Davis, Davis, CA 95616, USA.

4. Department of Applied Physics, Stanford University, Stanford, CA 94305, USA.

Abstract

Unwinding RNA for protein synthesis During the first steps of protein synthesis, the small subunit of the ribosome scans the 5′ end of the mRNA, looking for the protein start codon. This process involves one of the translation initiation factors, eIF4A, which helps to remove any RNA structures that might impede the ribosome's search. García-García et al. used single-molecule optical trap assays to show that eIF4A, in combination with two other translation initiation factors, is able to continuously and directionally unwind a double-stranded RNA hairpin. The factors unwound RNA in steps roughly equal to a turn of the RNA double helix. Science , this issue p. 1486

Funder

National Institute of General Medical Sciences

Alejandro and Lisa Zaffaroni Graduate Fellowship

Stanford Graduate Fellowship

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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