The Dbpa Catalytic Core Unwinds Double-Helix Substrates By Directly Loading On Them

Keywords

DbpA; DEAD-box protein; Ribosome assembly; Ribosome maturation factor; RNA helicase

Abstract

DbpA is a DEAD-box RNA helicase implicated in the assembly of the large ribosomal subunit. Similar to all the members of the DEAD-box family, the DbpA protein has two N-terminal RecA-like domains, which perform the RNA unwinding. However, unlike other members of this family, the DbpA protein also possesses a structured C-terminal RNA-binding domain that mediates specific tethering of DbpA to hairpin 92 of the Escherichia coli 23S ribosomal RNA. Previous studies using model RNA molecules containing hairpin 92 show that the RNA molecules support the DbpA protein's double-helix unwinding activity, provided that the double helix has a 3' single-stranded region. The 3' single-stranded region was suggested to be the start site of the DbpA protein's catalytic unwinding activity. The data presented here demonstrate that the single-stranded region 3' of the doublehelix substrate is not required for the DbpA protein's unwinding activity and the DbpA protein unwinds the double-helix substrates by directly loading on them.

Publication Date

3-1-2016

Publication Title

RNA

Volume

22

Issue

3

Number of Pages

408-415

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1261/rna.052928.115

Socpus ID

84958686442 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/84958686442

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