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

The tRNA<sup>His</sup> 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...

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Main Authors:	Allan W. Chen, Malithi I. Jayasinghe, Christina Z. Chung, Bhalchandra S. Rao, Rosan Kenana, Ilka U. Heinemann, Jane E. Jackman
Format:	Article
Language:	English
Published:	MDPI AG 2019-03-01
Series:	Genes
Subjects:	reverse polymerization tRNA editing tRNA repair protein engineering synthetic biology
Online Access:	https://www.mdpi.com/2073-4425/10/3/250

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spelling	doaj-eaefaf67fa2c4c67b1f48680d480bdc32020-11-25T00:55:53ZengMDPI AGGenes2073-44252019-03-0110325010.3390/genes10030250genes10030250The Role of 3′ to 5′ Reverse RNA Polymerization in tRNA Fidelity and RepairAllan W. Chen0Malithi I. Jayasinghe1Christina Z. Chung2Bhalchandra S. Rao3Rosan Kenana4Ilka U. Heinemann5Jane E. Jackman6Department of Biochemistry, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5C1, CanadaDepartment of Chemistry and Biochemistry, Center for RNA Biology, Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USADepartment of Biochemistry, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5C1, CanadaDepartment of Chemistry and Biochemistry, Center for RNA Biology, Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USADepartment of Biochemistry, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5C1, CanadaDepartment of Biochemistry, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5C1, CanadaDepartment of Chemistry and Biochemistry, Center for RNA Biology, Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USAThe tRNA<sup>His</sup> 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.https://www.mdpi.com/2073-4425/10/3/250reverse polymerizationtRNA editingtRNA repairprotein engineeringsynthetic biology
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Allan W. Chen Malithi I. Jayasinghe Christina Z. Chung Bhalchandra S. Rao Rosan Kenana Ilka U. Heinemann Jane E. Jackman
spellingShingle	Allan W. Chen Malithi I. Jayasinghe Christina Z. Chung Bhalchandra S. Rao Rosan Kenana Ilka U. Heinemann Jane E. Jackman The Role of 3′ to 5′ Reverse RNA Polymerization in tRNA Fidelity and Repair Genes reverse polymerization tRNA editing tRNA repair protein engineering synthetic biology
author_facet	Allan W. Chen Malithi I. Jayasinghe Christina Z. Chung Bhalchandra S. Rao Rosan Kenana Ilka U. Heinemann Jane E. Jackman
author_sort	Allan W. Chen
title	The Role of 3′ to 5′ Reverse RNA Polymerization in tRNA Fidelity and Repair
title_short	The Role of 3′ to 5′ Reverse RNA Polymerization in tRNA Fidelity and Repair
title_full	The Role of 3′ to 5′ Reverse RNA Polymerization in tRNA Fidelity and Repair
title_fullStr	The Role of 3′ to 5′ Reverse RNA Polymerization in tRNA Fidelity and Repair
title_full_unstemmed	The Role of 3′ to 5′ Reverse RNA Polymerization in tRNA Fidelity and Repair
title_sort	role of 3′ to 5′ reverse rna polymerization in trna fidelity and repair
publisher	MDPI AG
series	Genes
issn	2073-4425
publishDate	2019-03-01
description	The tRNA<sup>His</sup> 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.
topic	reverse polymerization tRNA editing tRNA repair protein engineering synthetic biology
url	https://www.mdpi.com/2073-4425/10/3/250
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The Role of 3′ to 5′ Reverse RNA Polymerization in tRNA Fidelity and Repair

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