Structural basis for tRNA methylthiolation by the radical SAM enzyme MiaB.

ABSTRACT: Numerous post-transcriptional modifications of transfer RNAs have vital roles in translation. The 2-methylthio-N⁶-isopentenyladenosine (ms²i⁶A) modification occurs at position 37 (A37) in transfer RNAs that contain adenine in position 36 of the anticodon, and serves to promote efficient A:U codon-anticodon base-pairing and to prevent unintended base pairing by near cognates, thus enhancing translational fidelity^1-4. The ms²i⁶A modification is installed onto isopentenyladenosine (i⁶A) by MiaB, a radical S-adenosylmethionine (SAM) methylthiotransferase. As a radical SAM protein, MiaB contains one [Fe₄S₄]_RS cluster used in the reductive cleavage of SAM to form a 5'-deoxyadenosyl 5'-ra

SUBMITTER: Esakova OA 

PROVIDER: S-EPMC9107155 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature