scholarly journals Functional analysis in Saccharomyces cerevisiae of naturally occurring amino acid substitutions in human dihydrolipoamide dehydrogenase

1996 ◽  
Vol 5 (10) ◽  
pp. 1643-1648 ◽  
Author(s):  
M. Lanterman
2010 ◽  
Vol 47 (5) ◽  
pp. 1023-1030 ◽  
Author(s):  
Diederik van de Wetering ◽  
Roelof A. de Paus ◽  
Jaap T. van Dissel ◽  
Esther van de Vosse

2017 ◽  
Vol 61 (5) ◽  
Author(s):  
Catiana Dudiuk ◽  
Daiana Macedo ◽  
Florencia Leonardelli ◽  
Laura Theill ◽  
Matias S. Cabeza ◽  
...  

ABSTRACT Candida guilliermondii shows intrinsic reduced echinocandin susceptibility. It harbors two polymorphisms (L633M and T634A) in the Fks1p hot spot 1 region. Our objective was to confirm that the reduced echinocandin susceptibility of C. guilliermondii is due to those naturally occurring substitutions. We constructed a Saccharomyces cerevisiae mutant in which a region of the FKS1 gene (including hot spot 1) was replaced with that from C. guilliermondii. The chimeric mutants showed 32-fold increases in echinocandin MIC values, confirming the hypothesis.


2017 ◽  
Vol 1859 (10) ◽  
pp. 2076-2085 ◽  
Author(s):  
Satoshi Uemura ◽  
Takahiro Mochizuki ◽  
Goyu Kurosaka ◽  
Takanori Hashimoto ◽  
Yuki Masukawa ◽  
...  

1990 ◽  
Vol 33 (7) ◽  
pp. 939-946 ◽  
Author(s):  
Xiaojiang Gao ◽  
Nancy J. Olsen ◽  
Theodore Pincus ◽  
Peter Stastny

2018 ◽  
Vol 62 (10) ◽  
Author(s):  
Kelley R. Healey ◽  
Milena Kordalewska ◽  
Cristina Jiménez Ortigosa ◽  
Ashutosh Singh ◽  
Indira Berrío ◽  
...  

ABSTRACTMultiple Erg11 amino acid substitutions were identified in clinical isolates ofCandida aurisoriginating from India and Colombia. Elevated azole MICs were detected inSaccharomyces cerevisiaeupon heterologous expression ofC. aurisERG11alleles that encoded for Y132F or K143R substitutions; however, expression of alleles encoding I466M, Y501H, or other clade-defined amino acid differences yielded susceptible MICs. Similar to otherCandidaspecies, specificC. aurisERG11mutations resulted directly in reduced azole susceptibility.


2000 ◽  
Vol 295 (4) ◽  
pp. 755-765 ◽  
Author(s):  
Vincent Parissi ◽  
Anne B Caumont ◽  
Vaea Richard de Soultrait ◽  
Christina Calmels ◽  
Sergio Pichuantes ◽  
...  

Genetics ◽  
1988 ◽  
Vol 120 (4) ◽  
pp. 923-934
Author(s):  
M G Sandbaken ◽  
M R Culbertson

Abstract A mutational analysis of the eukaryotic elongation factor EF-1 alpha indicates that this protein functions to limit the frequency of errors during genetic code translation. We found that both amino acid misincorporation and reading frame errors are controlled by EF-1 alpha. In order to examine the function of this protein, the TEF2 gene, which encodes EF-1 alpha in Saccharomyces cerevisiae, was mutagenized in vitro with hydroxylamine. Sixteen independent TEF2 alleles were isolated by their ability to suppress frameshift mutations. DNA sequence analysis identified eight different sites in the EF-1 alpha protein that elevate the frequency of mistranslation when mutated. These sites are located in two different regions of the protein. Amino acid substitutions located in or near the GTP-binding and hydrolysis domain of the protein cause suppression of frameshift and nonsense mutations. These mutations may effect mistranslation by altering the binding or hydrolysis of GTP. Amino acid substitutions located adjacent to a putative aminoacyl-tRNA binding region also suppress frameshift and nonsense mutations. These mutations may alter the binding of aminoacyl-tRNA by EF-1 alpha. The identification of frameshift and nonsense suppressor mutations in EF-1 alpha indicates a role for this protein in limiting amino acid misincorporation and reading frame errors. We suggest that these types of errors are controlled by a common mechanism or closely related mechanisms.


Sign in / Sign up

Export Citation Format

Share Document