The Role of 3' to 5' Reverse RNA Polymerization in tRNA Fidelity and Repair

Allan W Chen; Malithi I Jayasinghe; Christina Z Chung; Bhalchandra S Rao; Rosan Kenana; Ilka U Heinemann; Jane E Jackman

doi:10.3390/genes10030250

The Role of 3' to 5' Reverse RNA Polymerization in tRNA Fidelity and Repair

Genes (Basel). 2019 Mar 26;10(3):250. doi: 10.3390/genes10030250.

Authors

Allan W Chen¹, Malithi I Jayasinghe², Christina Z Chung³, Bhalchandra S Rao⁴, Rosan Kenana⁵, Ilka U Heinemann⁶, Jane E Jackman⁷

Affiliations

¹ Department of Biochemistry, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5C1, Canada. achen325@uwo.ca.
² Department of Chemistry and Biochemistry, Center for RNA Biology, Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. jayasinghearachchige.1@osu.edu.
³ Department of Biochemistry, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5C1, Canada. cchung88@uwo.ca.
⁴ Department of Chemistry and Biochemistry, Center for RNA Biology, Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. brao@arrakistx.com.
⁵ Department of Biochemistry, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5C1, Canada. rkenana@uwo.ca.
⁶ Department of Biochemistry, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5C1, Canada. ilka.heinemann@uwo.ca.com.
⁷ Department of Chemistry and Biochemistry, Center for RNA Biology, Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. Jackman.14@osu.edu.

Abstract

The tRNA^His guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity, which is the reverse of all other known DNA and RNA polymerases, makes this enzyme family a subject of biological and mechanistic interest. Previous biochemical, structural, and genetic investigations of multiple members of this family have revealed that Thg1 enzymes use the 3' to 5' chemistry for multiple reactions in biology. Here, we describe the current state of knowledge regarding the catalytic features and biological functions that have been so far associated with Thg1 and its homologs. Progress toward the exciting possibility of utilizing this unusual protein activity for applications in biotechnology is also discussed.

Keywords: protein engineering; reverse polymerization; synthetic biology; tRNA editing; tRNA repair.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

MeSH terms

DNA Repair
Nucleotidyltransferases / metabolism*
RNA, Transfer / metabolism*
Synthetic Biology

Substances

RNA, Transfer
Nucleotidyltransferases
guanylyltransferase

Abstract

Publication types

MeSH terms

Substances

Grants and funding