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In vitro substrate specificities of 3′–5′ polymerases correlate with biological outcomes of tRNA 5′‐editing reactions
Author(s) -
Long Yicheng,
Jackman Jane E.
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.06.028
Subject(s) - polymerase , transfer rna , biology , rna editing , organism , computational biology , nucleotidyltransferase , genetics , base pair , enzyme , biochemistry , rna , dna , gene
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.