An ancient type of MnmA protein is an iron-sulfur cluster-dependent sulfurtransferase for tRNA anticodons

Transfer RNA (tRNA) is an adaptor molecule indispensable for assigning amino acids to codons on mRNA during protein synthesis. 2-thiouridine (s U) derivatives in the anticodons (position 34) of tRNAs for glutamate, glutamine, and lysine are post-transcriptional modifications essential for precise an...

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Bibliographic Details
Published in:RNA (Cambridge) 2020-03, Vol.26 (3), p.240-250
Main Authors: Shigi, Naoki, Horitani, Masaki, Miyauchi, Kenjyo, Suzuki, Tsutomu, Kuroki, Misao
Format: Article
Language:English
Subjects:
Anaerobic conditions
Anticodon - genetics
Anticodons
Catalysis
Codon - genetics
Codons
Cyanobacteria
Cyanobacteria - genetics
Escherichia coli - genetics
Escherichia coli Proteins - genetics
Glutamic Acid - genetics
Glutamine
Glutamine - genetics
Iron
Iron - metabolism
Lysine
Lysine - genetics
Mitochondria
Mycobacterium - genetics
Post-transcription
Protein biosynthesis
RNA, Transfer - genetics
Spectroscopy
Sulfur
Sulfur - metabolism
Sulfurtransferase
Sulfurtransferases - chemistry
Sulfurtransferases - genetics
Thiouridine - analogs & derivatives
Thiouridine - metabolism
Transfer RNA
tRNA
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Summary:Transfer RNA (tRNA) is an adaptor molecule indispensable for assigning amino acids to codons on mRNA during protein synthesis. 2-thiouridine (s U) derivatives in the anticodons (position 34) of tRNAs for glutamate, glutamine, and lysine are post-transcriptional modifications essential for precise and efficient codon recognition in all organisms. s U34 is introduced either by (i) bacterial MnmA/eukaryote mitochondrial Mtu1 or (ii) eukaryote cytosolic Ncs6/archaeal NcsA, and the latter enzymes possess iron-sulfur (Fe-S) cluster. Here, we report the identification of novel-type MnmA homologs containing three conserved Cys residues, which could support Fe-S cluster binding and catalysis, in a broad range of bacteria, including thermophiles, , , , , and Using EPR spectroscopy, we revealed that MnmA (TtMnmA) contains an oxygen-sensitive [4Fe-4S]-type cluster. Efficient in vitro formation of s U34 in tRNA and tRNA by holo-TtMnmA occurred only under anaerobic conditions. Mutational analysis of TtMnmA suggested that the Fe-S cluster is coordinated by the three conserved Cys residues (Cys105, Cys108, and Cys200), and is essential for its activity. Evolutionary scenarios for the sulfurtransferases, including the Fe-S cluster containing Ncs6/NcsA s U thiouridylases and several distantly related sulfurtransferases, are proposed.
ISSN:1355-8382
1469-9001
DOI:10.1261/rna.072066.119