Dbpa Is A Region-Specific Rna Helicase

Keywords

ATPase; DEAD-box protein; ribosome maturation factor; RNA chaperone; RNA helicase

Abstract

DbpA is a DEAD-box RNA helicase implicated in RNA structural rearrangements in the peptidyl transferase center. DbpA contains an RNA binding domain, responsible for tight binding of DbpA to hairpin 92 of 23S ribosomal RNA, and a RecA-like catalytic core responsible for double-helix unwinding. It is not known if DbpA unwinds only the RNA helices that are part of a specific RNA structure, or if DbpA unwinds any RNA helices within the catalytic core's grasp. In other words, it is not known if DbpA is a site-specific enzyme or region-specific enzyme. In this study, we used protein and RNA engineering to investigate if DbpA is a region-specific or a site-specific enzyme. Our data suggest that DbpA is a region-specific enzyme. This conclusion has an important implication for the physiological role of DbpA. It suggests that during ribosome assembly, DbpA could bind with its C-terminal RNA binding domain to hairpin 92, while its catalytic core may unwind any double-helices in its vicinity. The only requirement for a double-helix to serve as a DbpA substrate is for the double-helix to be positioned within the catalytic core's grasp.

Publication Date

3-1-2017

Publication Title

Biopolymers

Volume

107

Issue

3

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1002/bip.23001

Socpus ID

85006744013 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/85006744013

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