Structural basis for tRNA methylthiolation by the radical SAM enzyme MiaB
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
https://www.nature.com/articles/s41586-021-03904-6.pdf
Reference42 articles.
1. Connolly, D. M. & Winkler, M. E. Genetic and physiological relationships among the miaA gene, 2-methylthio-N6-(delta 2-isopentenyl)-adenosine tRNA modification, and spontaneous mutagenesis in Escherichia coli K-12. J. Bacteriol. 171, 3233–3246 (1989).
2. Connolly, D. M. & Winkler, M. E. Structure of Escherichia coli K-12 miaA and characterization of the mutator phenotype caused by miaA insertion mutations. J. Bacteriol. 173, 1711–1721 (1991).
3. Esberg, B., Leung, H.-C. E., Tsui, H.-C. T., Björk, G. R. & Winkler, M. E. Identification of the miaB gene, involved in methylthiolation of isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and Escherichia coli. J. Bacteriol. 181, 7256–7265 (1999).
4. Urbonavicius, J., Qian, Q., Durand, J. M. B., Hagervall, T. G. & Björk, G. R. Improvement of reading frame maintenance is a common function for several tRNA modifications. EMBO J. 20, 4863–4873 (2001).
5. Arcinas, A. J. Mechanistic Studies of the Radical S-adenosyl-l-methionine (SAM) tRNA Methylthiotransferase MiaB. Ph.D. thesis, Pennsylvania State Univ., (2016).
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