Time Course Of Large Ribosomal Subunit Assembly In E. Coli Cells Overexpressing A Helicase Inactive Dbpa Protein

Keywords

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

Abstract

DbpA is a DEAD-box RNA helicase implicated in Escherichia coli large ribosomal subunit assembly. Previous studies have shown that when the ATPase and helicase inactive DbpA construct, R331A, is expressed in E. coli cells, a large ribosomal subunit intermediate accumulates. The large subunit intermediate migrates as a 45S particle in a sucrose gradient. Here, using a number of structural and fluorescent assays, we investigate the ribosome profiles of cells lacking wild-type DbpA and overexpressing the R331A DbpA construct. Our data show that in addition to the 45S particle previously described, 27S and 35S particles are also present in the ribosome profiles of cells overexpressing R331A DbpA. The 27S, 35S, and 45S independently convert to the 50S subunit, suggesting that ribosome assembly in the presence of R331A and the absence of wild-type DbpA occurs via multiple pathways.

Publication Date

7-1-2016

Publication Title

RNA

Volume

22

Issue

7

Number of Pages

1055-1064

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1261/rna.055137.115

Socpus ID

84975087357 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/84975087357

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