Identification of distinct biological functions for four 3′-5′ RNA polymerases
Author:
Publisher
Oxford University Press (OUP)
Subject
Genetics
Link
http://academic.oup.com/nar/article-pdf/44/17/8395/17438013/gkw681.pdf
Reference60 articles.
1. Post-transcriptional nucleotide addition is responsible for the formation of the 5' terminus of histidine tRNA.
2. Depletion of Saccharomyces cerevisiae tRNA His Guanylyltransferase Thg1p Leads to Uncharged tRNA His with Additional m 5 C
3. tRNAHis maturation: An essential yeast protein catalyzes addition of a guanine nucleotide to the 5′ end of tRNAHis
4. tRNAHis guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases
5. Structural Studies of a Bacterial tRNAHIS Guanylyltransferase (Thg1)-Like Protein, with Nucleotide in the Activation and Nucleotidyl Transfer Sites
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3. Fidelity of base-pair recognition by a 3′–5′ polymerase: mechanism of the Saccharomyces cerevisiae tRNAHis guanylyltransferase;RNA;2021-03-31
4. Analysis of GTP addition in the reverse (3′–5′) direction by human tRNAHis guanylyltransferase;RNA;2021-03-23
5. Unusual Occurrence of Two Bona-Fide CCA-Adding Enzymes in Dictyostelium discoideum;International Journal of Molecular Sciences;2020-07-23
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