Nonsynonymous Mutations in Linker-2 of the Pdr5 Multidrug Transporter Identify a New RNA Stability Element.
ABC transporter
Pdr5
drug resistance
mRNA
nonsynonymous mutation
Journal
G3 (Bethesda, Md.)
ISSN: 2160-1836
Titre abrégé: G3 (Bethesda)
Pays: England
ID NLM: 101566598
Informations de publication
Date de publication:
07 01 2020
07 01 2020
Historique:
pubmed:
24
11
2019
medline:
9
6
2020
entrez:
24
11
2019
Statut:
epublish
Résumé
Analysis of synonymous mutations established that although the primary amino acid sequence remains unchanged, alterations in transcription and translation can result in significant phenotypic consequences. We report the novel observation that a series of nonsynonymous mutations in an unconserved stretch of amino acids found in the yeast multidrug efflux pump Pdr5 increases expression, thus enhancing multidrug resistance. Cycloheximide chase experiments ruled out the possibility that the increased steady-state level of Pdr5 was caused by increased protein stability. Quantitative-RT PCR experiments demonstrated that the mutants had levels of
Identifiants
pubmed: 31757931
pii: g3.119.400863
doi: 10.1534/g3.119.400863
pmc: PMC6945031
doi:
Substances chimiques
ATP-Binding Cassette Transporters
0
PDR5 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, N.I.H., Intramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
357-369Subventions
Organisme : NIGMS NIH HHS
ID : R15 GM077211
Pays : United States
Informations de copyright
Copyright © 2020 Rahman et al.
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