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tRNA 5'-end repair activities of tRNAHis guanylyltransferase (Thg1)-like proteins from Bacteria and Archaea.
Rao BS, Maris EL, Jackman JE. Rao BS, et al. Nucleic Acids Res. 2011 Mar;39(5):1833-42. doi: 10.1093/nar/gkq976. Epub 2010 Nov 3. Nucleic Acids Res. 2011. PMID: 21051361 Free PMC article.
The tRNA(His) guanylyltransferase (Thg1) family comprises a set of unique 3'-5' nucleotide addition enzymes found ubiquitously in Eukaryotes, where they function in the critical G(-1) addition reaction required for tRNA(His) maturation. However, in most Bacteria and Archae …
The tRNA(His) guanylyltransferase (Thg1) family comprises a set of unique 3'-5' nucleotide addition enzymes found ubiquitously in Euk …
Human Thg1 displays tRNA-inducible GTPase activity.
Antika TR, Nazilah KR, Lee YH, Lo YT, Yeh CS, Yeh FL, Chang TH, Wang TL, Wang CC. Antika TR, et al. Nucleic Acids Res. 2022 Sep 23;50(17):10015-10025. doi: 10.1093/nar/gkac768. Nucleic Acids Res. 2022. PMID: 36107775 Free PMC article.
tRNAHis guanylyltransferase (Thg1) catalyzes the 3'-5' incorporation of guanosine into position -1 (G-1) of tRNAHis. ...Yeast Thg1 requires ATP for G-1 addition to tRNAHis opposite A73, whereas archaeal Thg1 requires either ATP or GTP for …
tRNAHis guanylyltransferase (Thg1) catalyzes the 3'-5' incorporation of guanosine into position -1 (G-1) of tRNAHis. .. …
tRNAHis-guanylyltransferase establishes tRNAHis identity.
Heinemann IU, Nakamura A, O'Donoghue P, Eiler D, Söll D. Heinemann IU, et al. Nucleic Acids Res. 2012 Jan;40(1):333-44. doi: 10.1093/nar/gkr696. Epub 2011 Sep 2. Nucleic Acids Res. 2012. PMID: 21890903 Free PMC article.
Histidine transfer RNA (tRNA) is unique among tRNA species as it carries an additional nucleotide at its 5' terminus. ...Yeast Thg1 displays a unique but limited ability to add 2-3 G or C residues to mutant tRNA substrates, thus catalyzing a 3' 5' RNA …
Histidine transfer RNA (tRNA) is unique among tRNA species as it carries an additional nucleotide at its 5' terminus. ...Yeast …
Minimal requirements for reverse polymerization and tRNA repair by tRNAHis guanylyltransferase.
Desai R, Kim K, Büchsenschütz HC, Chen AW, Bi Y, Mann MR, Turk MA, Chung CZ, Heinemann IU. Desai R, et al. RNA Biol. 2018;15(4-5):614-622. doi: 10.1080/15476286.2017.1372076. Epub 2017 Sep 29. RNA Biol. 2018. PMID: 28901837 Free PMC article.
These enzymes normally catalyze a single 5' guanylation of tRNA(His) lacking the essential G(-1) identity element required for aminoacylation. Recent studies suggest that archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes is phylogenetically …
These enzymes normally catalyze a single 5' guanylation of tRNA(His) lacking the essential G(-1) identity element required for aminoacylatio …
Doing it in reverse: 3'-to-5' polymerization by the Thg1 superfamily.
Jackman JE, Gott JM, Gray MW. Jackman JE, et al. RNA. 2012 May;18(5):886-99. doi: 10.1261/rna.032300.112. Epub 2012 Mar 28. RNA. 2012. PMID: 22456265 Free PMC article. Review.
The tRNA(His) guanylyltransferase (Thg1) family of enzymes comprises members from all three domains of life (Eucarya, Bacteria, Archaea). ...Here we review recent advances toward understanding diverse Thg1 family enzyme functions and mechanisms. We also discuss poss …
The tRNA(His) guanylyltransferase (Thg1) family of enzymes comprises members from all three domains of life (Eucarya, Bacteria, Archa …
The requirement for the highly conserved G-1 residue of Saccharomyces cerevisiae tRNAHis can be circumvented by overexpression of tRNAHis and its synthetase.
Preston MA, Phizicky EM. Preston MA, et al. RNA. 2010 May;16(5):1068-77. doi: 10.1261/rna.2087510. Epub 2010 Apr 1. RNA. 2010. PMID: 20360392 Free PMC article.
However, the essential roles of Thg1 are unclear since Thg1 also interacts with Orc2 of the origin recognition complex, is implicated in the cell cycle, and catalyzes an unusual template-dependent 3'-5' (reverse) polymerization in vitro at the 5' end of activated tR …
However, the essential roles of Thg1 are unclear since Thg1 also interacts with Orc2 of the origin recognition complex, is imp …
The Role of 3' to 5' Reverse RNA Polymerization in tRNA Fidelity and Repair.
Chen AW, Jayasinghe MI, Chung CZ, Rao BS, Kenana R, Heinemann IU, Jackman JE. Chen AW, et al. Genes (Basel). 2019 Mar 26;10(3):250. doi: 10.3390/genes10030250. Genes (Basel). 2019. PMID: 30917604 Free PMC article. Review.
The tRNA(His) 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 …
The tRNA(His) guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the …
Fidelity of base-pair recognition by a 3'-5' polymerase: mechanism of the Saccharomyces cerevisiae tRNAHis guanylyltransferase.
Patel KJ, Yourik P, Jackman JE. Patel KJ, et al. RNA. 2021 Jun;27(6):683-693. doi: 10.1261/rna.078686.121. Epub 2021 Mar 31. RNA. 2021. PMID: 33790044 Free PMC article.
Subsequent investigation revealed an entire class of enzymes related to Thg1, called Thg1-like proteins (TLPs). TLPs are found in all three domains of life and preferentially catalyze 3'-5' polymerase activity, utilizing this unusual activity to repair tRNA, among o …
Subsequent investigation revealed an entire class of enzymes related to Thg1, called Thg1-like proteins (TLPs). TLPs are found …
3'-5' tRNAHis guanylyltransferase in bacteria.
Heinemann IU, Randau L, Tomko RJ Jr, Söll D. Heinemann IU, et al. FEBS Lett. 2010 Aug 20;584(16):3567-72. doi: 10.1016/j.febslet.2010.07.023. Epub 2010 Jul 23. FEBS Lett. 2010. PMID: 20650272 Free PMC article.
The identity of the histidine specific transfer RNA (tRNA(His)) is largely determined by a unique guanosine residue at position -1. ...Here, we show that Thg1 also occurs in bacteria. We demonstrate in vitro Thg1 activity for recombinant enzymes from t …
The identity of the histidine specific transfer RNA (tRNA(His)) is largely determined by a unique guanosine residue at positio …
Kinetic analysis of 3'-5' nucleotide addition catalyzed by eukaryotic tRNA(His) guanylyltransferase.
Smith BA, Jackman JE. Smith BA, et al. Biochemistry. 2012 Jan 10;51(1):453-65. doi: 10.1021/bi201397f. Epub 2011 Dec 14. Biochemistry. 2012. PMID: 22136300 Free PMC article.
The tRNA(His) guanylyltransferase (Thg1) catalyzes the incorporation of a single guanosine residue at the -1 position (G(-1)) of tRNA(His), using an unusual 3'-5' nucleotidyl transfer reaction. ...The high-resolution crystal structure of human Thg1 revealed r …
The tRNA(His) guanylyltransferase (Thg1) catalyzes the incorporation of a single guanosine residue at the -1 position (G(-1)) of tRNA …
37 results