The Universal YrdC/Sua5 Family is Required for the Formation of Threonylcarbamoyladenosine in TRNA

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 2009 Mar 17

PMID 19287007

Citations 110

Authors

Basma El Yacoubi

Benjamin Lyons

Yulien Cruz

Robert Reddy

Brian Nordin

Fabio Agnelli

James R Williamson

Paul Schimmel

Manal A Swairjo

Valerie de Crecy-Lagard

Affiliations

Soon will be listed here.

Abstract

Threonylcarbamoyladenosine (t(6)A) is a universal modification found at position 37 of ANN decoding tRNAs, which imparts a unique structure to the anticodon loop enhancing its binding to ribosomes in vitro. Using a combination of bioinformatic, genetic, structural and biochemical approaches, the universal protein family YrdC/Sua5 (COG0009) was shown to be involved in the biosynthesis of this hypermodified base. Contradictory reports on the essentiality of both the yrdC wild-type gene of Escherichia coli and the SUA5 wild-type gene of Saccharomyces cerevisiae led us to reconstruct null alleles for both genes and prove that yrdC is essential in E. coli, whereas SUA5 is dispensable in yeast but results in severe growth phenotypes. Structural and biochemical analyses revealed that the E. coli YrdC protein binds ATP and preferentially binds RNA(Thr) lacking only the t(6)A modification. This work lays the foundation for elucidating the function of a protein family found in every sequenced genome to date and understanding the role of t(6)A in vivo.

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