Abstract
Protozoan mitochondrial tRNAs (mt-tRNAs) are repaired by a process known as 5'-editing. Mt-tRNA sequencing revealed organism-specific patterns of editing G-U base pairs, wherein some species remove G-U base pairs during 5'-editing, while others retain G-U pairs in the edited tRNA. We tested whether 3'-5' polymerases that catalyze the repair step of 5'-editing exhibit organism-specific preferences that explain the treatment of G-U base pairs. Biochemical and kinetic approaches revealed that a 3'-5' polymerase from Acanthamoeba castellanii tolerates G-U wobble pairs in editing substrates much more readily than several other enzymes, consistent with its biological pattern of editing.
Keywords:
3′–5′ polymerase; Acanthamoeba castellanii; Dictyostelium discoideum; Mitochondrial tRNA; Thg1-like protein; tRNA editing.
Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Comparative Study
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Acanthamoeba castellanii / enzymology*
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Acanthamoeba castellanii / metabolism
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Dictyostelium / enzymology
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Dictyostelium / metabolism
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Electrophoresis, Polyacrylamide Gel
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Isoenzymes / genetics
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Isoenzymes / metabolism
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Isotope Labeling
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Kinetics
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Mitochondria / enzymology*
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Mitochondria / metabolism
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Models, Molecular
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Phosphorus Radioisotopes
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Protozoan Proteins / genetics
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Protozoan Proteins / metabolism*
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RNA Editing*
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RNA Nucleotidyltransferases / genetics
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RNA Nucleotidyltransferases / metabolism*
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RNA, Protozoan / chemistry
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RNA, Protozoan / metabolism*
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RNA, Transfer / chemistry
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RNA, Transfer / metabolism*
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RNA, Transfer, Ile / chemistry
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RNA, Transfer, Ile / metabolism
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Recombinant Proteins / metabolism
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Species Specificity
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Substrate Specificity
Substances
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Isoenzymes
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Phosphorus Radioisotopes
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Protozoan Proteins
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RNA, Protozoan
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RNA, Transfer, Ile
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Recombinant Proteins
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RNA, Transfer
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RNA Nucleotidyltransferases
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tRNA nucleotidyltransferase