Literature summary for 2.7.1.160 extracted from

Cherry, P.D.; White, L.K.; York, K.; Hesselberth, J.R.
Genetic bypass of essential RNA repair enzymes in budding yeast (2018), RNA, 24, 313-323 .

Search for more literature for 2.7.1.160

Protein Variants

Protein Variants	Comment	Organism
additional information	generation and analysis of diverse mutant strains derived from Saccharomyces cerevisiae strain W303. The essential functions of TRL1 and TPT1 in budding yeast are bypassed by expressing prespliced, intronless versions of the 10 normally intron-containing tRNAs, indicating this repair pathway does not have additional essential functions. Expression of intronless tRNAs fails to rescue the growth of cells with deletions in components of the SEN complex, implying an additional essential role for the splicing endonuclease. The trl1DELTA and tpt1DELTA mutants accumulate tRNA and HAC1 splicing intermediates indicative of RNA repair defects and are hypersensitive to drugs that inhibit translation. tpt1DELTA mutants grow in the presence of tunicamycin despite reduced accumulation of spliced HAC1 mRNA, while failure to induce the unfolded protein response occurs in trl1DELTA cells grown with tunicamycin is lethal owing to their inability to ligate HAC1 after its cleavage by Ire1. Tpt1DELTA phenotype, overview	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2'-phospho-[ligated tRNA] + NAD+	Saccharomyces cerevisiae	-	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	Q12272	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2'-phospho-[ligated tRNA] + NAD+	-	Saccharomyces cerevisiae	mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide	-	?

Synonyms

Synonyms	Comment	Organism
Tpt1	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
malfunction	the essential functions of TRL1 and TPT1 in budding yeast are bypassed by expressing prespliced, intronless versions of the 10 normally intron-containing tRNAs, indicating this repair pathway does not have additional essential functions. Expression of intronless tRNAs fails to rescue the growth of cells with deletions in components of the SEN complex, implying an additional essential role for the splicing endonuclease. The trl1DELTA and tpt1DELTA mutants accumulate tRNA and HAC1 splicing intermediates indicative of RNA repair defects and are hypersensitive to drugs that inhibit translation. RNA repair mutants have defects in translation. tpt1DELTA mutants grow in the presence of tunicamycin despite reduced accumulation of spliced HAC1 mRNA, while failure to induce the unfolded protein response occurs in trl1DELTA cells grown with tunicamycin is lethal owing to their inability to ligate HAC1 after its cleavage by Ire1. Rescued trl1DELTA and tpt1DELTA cells, RNA repair mutants, have unique phenotypes for both tRNA splicing and HAC1 mRNA splicing during the unfolded protein response. The temperature sensitivity of RNA repair mutants at 37°C is not a consequence of tRNA decay pathway (RTD)	Saccharomyces cerevisiae
metabolism	RNA repair enzymes catalyze rejoining of an RNA molecule after cleavage of phosphodiester linkages. RNA repair in budding yeast is catalyzed by two separate enzymes that process tRNA exons during their splicing and HAC1 mRNA exons during activation of the unfolded protein response (UPR). The RNA ligase Trl1 (EC 6.5.1.3) joins 2',3'-cyclic phosphate and 5'-hydroxyl RNA fragments, creating a phosphodiester linkage with a 2'-phosphate at the junction. The 2'-phosphate is removed by the 2'-phosphotransferase Tpt1 (EC 2.7.1.160)	Saccharomyces cerevisiae
physiological function	enzyme TPT1 is essential only in the context of the generation of 2'-phosphorylated tRNAs by Trl1	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)