The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA

Threonylcarbamoyladenosine (t6A) 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 unive...

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Bibliographic Details
Published in:Nucleic acids research 2009-05, Vol.37 (9), p.2894-2909
Main Authors: El Yacoubi, Basma, Lyons, Benjamin, Cruz, Yulien, Reddy, Robert, Nordin, Brian, Agnelli, Fabio, Williamson, James R., Schimmel, Paul, Swairjo, Manal A., de Crécy-Lagard, Valérie
Format: Article
Language:English
Subjects:
Adenosine - analogs & derivatives
Adenosine - biosynthesis
Adenosine Triphosphate - metabolism
Amino Acid Sequence
DNA-Binding Proteins - genetics
Escherichia coli
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Genes, Essential
Genomics
Molecular Sequence Data
RNA
RNA, Transfer - chemistry
RNA, Transfer - metabolism
RNA, Transfer, Thr - chemistry
RNA, Transfer, Thr - metabolism
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins - genetics
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Summary:Threonylcarbamoyladenosine (t6A) 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 RNAThr lacking only the t6A 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 t6A in vivo.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkp152