| dc.creator | Großhans, H. | en |
| dc.creator | Lecointe, F. | en |
| dc.creator | Grosjean, H. | en |
| dc.creator | Hurt, E. | en |
| dc.creator | Simos, G. | en |
| dc.date.accessioned | 2015-11-23T10:29:16Z | |
| dc.date.available | 2015-11-23T10:29:16Z | |
| dc.date.issued | 2001 | |
| dc.identifier | 10.1074/jbc.M107141200 | |
| dc.identifier.issn | 219258 | |
| dc.identifier.uri | http://hdl.handle.net/11615/28240 | |
| dc.description.abstract | Yeast Pus1p catalyzes the formation of pseudouridine (ψ) at specific sites of several tRNAs, but its function is not essential for cell viability. We show here that Pus1p becomes essential when another tRNA: pseudouridine synthase, Pus4p, or the essential minor tRNA for glutamine are mutated. Strikingly, this mutant tRNA, which carries a mismatch in the TψC arm, displays a nuclear export defect. Furthermore, nuclear export of at least one wild-type tRNA species becomes defective in the absence of Pus1p. Our data, thus, show that the modifications formed by Pus1p are essential when other aspects of tRNA biogenesis or function are compromised and suggest that impairment of nuclear tRNA export in the absence of Pus1p might contribute to this phenotype. | en |
| dc.source.uri | http://www.scopus.com/inward/record.url?eid=2-s2.0-0035824521&partnerID=40&md5=466b546f0c5f31b42aa4bdcce567d6f3 | |
| dc.subject | Catalysis | en |
| dc.subject | RNA | en |
| dc.subject | Biogenesis | en |
| dc.subject | Yeast | en |
| dc.subject | fungal protein | en |
| dc.subject | glutamine | en |
| dc.subject | protein pus1p | en |
| dc.subject | protein pus4p | en |
| dc.subject | pseudouridine synthase | en |
| dc.subject | synthetase | en |
| dc.subject | transfer RNA | en |
| dc.subject | unclassified drug | en |
| dc.subject | fungal RNA | en |
| dc.subject | Hydro Lyases | en |
| dc.subject | hydrolyase | en |
| dc.subject | primer DNA | en |
| dc.subject | pseudouridine | en |
| dc.subject | pseudouridylate synthetase | en |
| dc.subject | animal cell | en |
| dc.subject | article | en |
| dc.subject | binding site | en |
| dc.subject | cell viability | en |
| dc.subject | controlled study | en |
| dc.subject | mismatch repair | en |
| dc.subject | nonhuman | en |
| dc.subject | phenotype | en |
| dc.subject | priority journal | en |
| dc.subject | protein modification | en |
| dc.subject | pseudouridinylation | en |
| dc.subject | reaction analysis | en |
| dc.subject | RNA analysis | en |
| dc.subject | wild type | en |
| dc.subject | biosynthesis | en |
| dc.subject | enzymology | en |
| dc.subject | genetic complementation | en |
| dc.subject | genetics | en |
| dc.subject | metabolism | en |
| dc.subject | mutation | en |
| dc.subject | nucleotide sequence | en |
| dc.subject | Saccharomyces cerevisiae | en |
| dc.subject | transport at the cellular level | en |
| dc.subject | Animalia | en |
| dc.subject | Base Sequence | en |
| dc.subject | Biological Transport | en |
| dc.subject | DNA Primers | en |
| dc.subject | Genetic Complementation Test | en |
| dc.subject | Hydro-Lyases | en |
| dc.subject | RNA, Fungal | en |
| dc.subject | RNA, Transfer | en |
| dc.subject | Support, Non-U.S. Gov't | en |
| dc.title | Pus1p-dependent tRNA Pseudouridinylation Becomes Essential When tRNA Biogenesis Is Compromised in Yeast | en |
| dc.type | journalArticle | en |