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The conformational plasticity of eukaryotic RNA ‐dependent ATP ases
Author(s) -
Ozgur Sevim,
Buchwald Gretel,
Falk Sebastian,
Chakrabarti Sutapa,
Prabu Jesuraj Rajan,
Conti Elena
Publication year - 2015
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13198
Subject(s) - helicase , rna , biology , microbiology and biotechnology , eif4a , transcription (linguistics) , biochemistry , homologous recombination , effector , nucleic acid , chemistry , non coding rna , dna , gene , linguistics , philosophy
RNA helicases are present in all domains of life and participate in almost all aspects of RNA metabolism, from transcription and processing to translation and decay. The diversity of pathways and substrates that they act on is reflected in the diversity of their individual functions, structures, and mechanisms. However, RNA helicases also share hallmark properties. At the functional level, they promote rearrangements of RNA s and RNP particles by coupling nucleic acid binding and release with ATP hydrolysis. At the molecular level, they contain two domains homologous to the bacterial RecA recombination protein. This conserved catalytic core is flanked by additional domains, which typically regulate the ATP ase activity in cis. Binding to effector proteins targets or regulates the ATP ase activity in trans. Structural and biochemical studies have converged on the plasticity of RNA helicases as a fundamental property that is used to control their timely activation in the cell. In this review, we focus on the conformational regulation of conserved eukaryotic RNA helicases.