Strictly Conserved Lysine of Prolyl-tRNA Synthetase Editing Domain Facilitates Binding and Positioning of Misacylated tRNAPro-Reference-Cited by-同舟云学术

Strictly Conserved Lysine of Prolyl-tRNA Synthetase Editing Domain Facilitates Binding and Positioning of Misacylated tRNAPro

Published:2014-02-03 Issue:6 Volume:53 Page:1059-1068
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Bartholow Thomas G.¹,Sanford Brianne L.²,Cao Bach¹,Schmit Heidi L.¹,Johnson James M.¹,Meitzner Jet¹,Bhattacharyya Sudeep¹,Musier-Forsyth Karin²,Hati Sanchita¹

Affiliation:

1. Department of Chemistry, University of Wisconsin-Eau Claire, Eau Claire, Wisconsin, 54702, United States

2. Department of Chemistry and Biochemistry, Center for RNA Biology, The Ohio State University, Columbus, Ohio, 43210, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi401279r

Reference54 articles.

1. Hydrolytic editing by a class II aminoacyl-tRNA synthetase

2. Cysteine Activation Is an Inherent in Vitro Property of Prolyl-tRNA Synthetases

3. Pre-transfer Editing by Class II Prolyl-tRNA Synthetase

4. Functional Role of the Prokaryotic Proline-tRNA Synthetase Insertion Domain in Amino Acid Editing

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