Kinetics And Thermodynamics Of Dbpa Protein'S C-Terminal Domain Interaction With Rna

Abstract

DbpA is an Escherichia coli DEAD-box RNA helicase implicated in RNA structural isomerization in the peptide bond formation site. In addition to the RecA-like catalytic core conserved in all of the members of DEAD-box family, DbpA contains a structured C-terminal domain, which is responsible for anchoring DbpA to hairpin 92 of 23S ribosomal RNA during the ribosome assembly process. Here, surface plasmon resonance was used to determine the equilibrium dissociation constant and the microscopic rate constants of the DbpA C-terminal domain association and dissociation to a fragment of 23S ribosomal RNA containing hairpin 92. Our results show that the DbpA protein's residence time on the RNA is 10 times longer than the time DbpA requires to hydrolyze one ATP. Thus, our data suggest that once bound to the intermediate ribosomal particles via its RNA-binding domain, DbpA could unwind a number of double-helix substrates before its dissociation from the ribosomal particles.

Publication Date

11-30-2017

Publication Title

ACS Omega

Volume

2

Issue

11

Number of Pages

8033-8038

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1021/acsomega.7b01205

Socpus ID

85052558190 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/85052558190

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