scholarly journals Functional Characterization of Individual- and Mixed-Burgundian Saccharomyces cerevisiae Isolates for Fermentation of Pinot Noir

Molecules ◽  
2015 ◽  
Vol 20 (3) ◽  
pp. 5112-5136 ◽  
Author(s):  
Emily Terrell ◽  
Margaret Cliff ◽  
Hennie Van Vuuren
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Functional Characterization ◽  
Pinot Noir

Isolation and functional characterization of mutant ferrochelatases in Saccharomyces cerevisiae

Biochimie ◽  
1996 ◽  
Vol 78 (2) ◽  
pp. 144-152 ◽  
Author(s):  
M. Góra ◽  
A. Chaciñska ◽  
J. Rytka ◽  
R. Labbe-Bois
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Functional Characterization

Use of Monoclonal Antibodies in the Functional Characterization of the Saccharomyces Cerevisiae Sepl Protein

1995 ◽  
Vol 231 (2) ◽  
pp. 329-336 ◽  
Author(s):  
Anita Holler ◽  
Vladimir I. Bashkirov ◽  
Jachen A. Solinger ◽  
Ursula Reinhart ◽  
Wolf-Dietrich Heyer
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Monoclonal Antibodies ◽  
Functional Characterization

scholarly journals Functional Characterization of Pneumocystis carinii brl1 by Transspecies Complementation Analysis

2007 ◽  
Vol 6 (12) ◽  
pp. 2448-2452 ◽  
Author(s):  
Libera Lo Presti ◽  
Moira Cockell ◽  
Lorenzo Cerutti ◽  
Viesturs Simanis ◽  
Philippe M. Hauser
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Membrane Proteins ◽  
Nuclear Membrane ◽  
Opportunistic Infections ◽  
Functional Characterization ◽  
Pneumocystis Carinii ◽  
Ectopic Expression ◽  
Functional Complementation ◽  
Null Alleles

ABSTRACT Pneumocystis jirovecii is a fungus which causes severe opportunistic infections in immunocompromised humans. The brl1 gene of P. carinii infecting rats was identified and characterized by using bioinformatics in conjunction with functional complementation in Saccharomyces cerevisiae and Schizosaccharomyces pombe. The ectopic expression of this gene rescues null alleles of essential nuclear membrane proteins of the Brr6/Brl1 family in both yeasts.

scholarly journals Functional characterization of Ost3p. Loss of the 34-kD subunit of the Saccharomyces cerevisiae oligosaccharyltransferase results in biased underglycosylation of acceptor substrates.

1995 ◽  
Vol 130 (3) ◽  
pp. 567-577 ◽  
Author(s):  
D Karaoglu ◽  
D J Kelleher ◽  
R Gilmore
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Functional Characterization ◽  
Null Mutant ◽  
Wild Type ◽  
Membrane Glycoproteins ◽  
En Bloc ◽  
Oligosaccharide Moiety

Within the lumen of the rough endoplasmic reticulum, oligosaccharyltransferase catalyzes the en bloc transfer of a high mannose oligosaccharide moiety from the lipid-linked oligosaccharide donor to asparagine acceptor sites in nascent polypeptides. The Saccharomyces cerevisiae oligosaccharyltransferase was purified as a heteroligomeric complex consisting of six subunits (alpha-zeta) having apparent molecular masses of 64 kD (Ost1p), 45 kD (Wbp1p), 34 kD, 30 kD (Swp1p), 16 kD, and 9 kD. Here we report a structural and functional characterization of Ost3p which corresponds to the 34-kD gamma-subunit of the oligosaccharyltransferase. Unlike Ost1p, Wbp1p, and Swp1p, expression of Ost3p is not essential for viability of yeast. Instead, ost3 null mutant yeast grow at wild-type rates on solid or in liquid media irrespective of culture temperature. Nonetheless, detergent extracts prepared from ost3 null mutant membranes are twofold less active than extracts prepared from wild-type membranes in an in vitro oligosaccharyltransferase assay. Furthermore, loss of Ost3p is accompanied by significant underglycosylation of soluble and membrane-bound glycoproteins in vivo. Compared to the previously characterized ost1-1 mutant in the oligosaccharyltransferase, and the alg5 mutant in the oligosaccharide assembly pathway, ost3 null mutant yeast appear to be selectively impaired in the glycosylation of several membrane glycoproteins. The latter observation suggests that Ost3p may enhance oligosaccharide transfer in vivo to a subset of acceptor substrates.

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