scholarly journals Improving the activity of endoglucanase I (EGI) from Saccharomyces cerevisiae by DNA shuffling

RSC Advances ◽  
2017 ◽  
Vol 7 (73) ◽  
pp. 46246-46256 ◽  
Author(s):  
Xu Wang ◽  
Liang Rong ◽  
Mingfu Wang ◽  
Yingjie Pan ◽  
Yong Zhao ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Trichoderma Reesei ◽  
Dna Shuffling ◽  
Glucanase Activity ◽  
Trichoderma Longibrachiatum ◽  
Trichoderma Pseudokoningii ◽  
Encoding Gene ◽  
Endoglucanase I

To enhance the endo-β-1,4-glucanase activity of three mixedTrichodermasp. (Trichoderma reesei, Trichoderma longibrachiatum, andTrichoderma pseudokoningii), we optimized the efficiency of the encoding gene using DNA shuffling andSaccharomyces cerevisiaeINVSc1 as a host.

Cloning, Characterization and Expression in Saccharomyces Cerevisiae of Endoglucanase I from Trichoderma Reesei

1987 ◽  
Vol 5 (1) ◽  
pp. 60-64 ◽  
Author(s):  
Janelle N. Van Arsdell ◽  
Shirley Kwok ◽  
Vicki L. Schweickart ◽  
Martha B. Ladner ◽  
David H. Gelfand ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Trichoderma Reesei ◽  
Endoglucanase I

scholarly journals Expression of an ATP-binding cassette transporter-encoding gene (YOR1) is required for oligomycin resistance in Saccharomyces cerevisiae.

1995 ◽  
Vol 15 (12) ◽  
pp. 6875-6883 ◽  
Author(s):  
D J Katzmann ◽  
T C Hallstrom ◽  
M Voet ◽  
W Wysock ◽  
J Golin ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fusion Gene ◽  
Sequence Similarity ◽  
Yeast Cells ◽  
Atp Binding ◽  
Zinc Cluster ◽  
Atp Binding Cassette Transporter ◽  
Transporter Family ◽  
Encoding Gene ◽  
Atp Binding Cassette

Semidominant mutations in the PDR1 or PDR3 gene lead to elevated resistance to cycloheximide and oligomycin. PDR1 and PDR3 have been demonstrated to encode zinc cluster transcription factors. Cycloheximide resistance mediated by PDR1 and PDR3 requires the presence of the PDR5 membrane transporter-encoding gene. However, PDR5 is not required for oligomycin resistance. Here, we isolated a gene that is necessary for PDR1- and PDR3-mediated oligomycin resistance. This locus, designated YOR1, causes a dramatic elevation in oligomycin resistance when present in multiple copies. A yor1 strain exhibits oligomycin hypersensitivity relative to an isogenic wild-type strain. In addition, loss of the YOR1 gene blocks the elevation in oligomycin resistance normally conferred by mutant forms of PDR1 or PDR3. The YOR1 gene product is predicted to be a member of the ATP-binding cassette transporter family of membrane proteins. Computer alignment indicates that Yor1p shows striking sequence similarity with multidrug resistance-associated protein, Saccharomyces cerevisiae Ycf1p, and the cystic fibrosis transmembrane conductance regulator. Use of a YOR1-lacZ fusion gene indicates that YOR1 expression is responsive to PDR1 and PDR3. While PDR5 expression is strictly dependent on the presence of PDR1 or PDR3, control of YOR1 expression has a significant PDR1/PDR3-independent component. Taken together, these data indicate that YOR1 provides the link between transcriptional regulation by PDR1 and PDR3 and oligomycin resistance of yeast cells.

scholarly journals The immunosuppressant SR 31747 blocks cell proliferation by inhibiting a steroid isomerase in Saccharomyces cerevisiae.

1996 ◽  
Vol 16 (6) ◽  
pp. 2719-2727 ◽  
Author(s):  
S Silve ◽  
P Leplatois ◽  
A Josse ◽  
P H Dupuy ◽  
C Lanau ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Proliferation ◽  
Gene Product ◽  
In Vitro Assays ◽  
Gene Products ◽  
Yeast Saccharomyces Cerevisiae ◽  
Isomerase Activity ◽  
Encoding Gene ◽  
Resistant Mutants

SR 31747 is a novel immunosuppressant agent that arrests cell proliferation in the yeast Saccharomyces cerevisiae, SR 31747-treated cells accumulate the same aberrant sterols as those found in a mutant impaired in delta 8- delta 7-sterol isomerase. Sterol isomerase activity is also inhibited by SR 31747 in in vitro assays. Overexpression of the sterol isomerase-encoding gene, ERG2, confers enhanced SR resistance. Cells growing anaerobically on ergosterol-containing medium are not sensitive to SR. Disruption of the sterol isomerase-encoding gene is lethal in cells growing in the absence of exogenous ergosterol, except in SR-resistant mutants lacking either the SUR4 or the FEN1 gene product. The results suggest that sterol isomerase is the target of SR 31747 and that both the SUR4 and FEN1 gene products are required to mediate the proliferation arrest induced by ergosterol depletion.

Cloning and sequencing of the GMP synthetase-encoding gene of Saccharomyces cerevisiae

Gene ◽  
1994 ◽  
Vol 139 (1) ◽  
pp. 127-132 ◽  
Author(s):  
Geneviève Dujardin ◽  
Michèle Kermorgant ◽  
Piotr P. Slonimski ◽  
Hélian Boucherie
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cloning And Sequencing ◽  
Encoding Gene ◽  
Gmp Synthetase

scholarly journals Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in Saccharomyces cerevisiae

2020 ◽  
Vol 21 (23) ◽  
pp. 8938
Author(s):  
Sebastian Piłsyk ◽  
Urszula Perlinska-Lenart ◽  
Anna Janik ◽  
Elżbieta Gryz ◽  
Marta Ajchler-Adamska ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Functional Analysis ◽  
Trichoderma Reesei ◽  
Transmembrane Domain ◽  
Human Cells ◽  
Catalytic Subunit ◽  
Yeast Saccharomyces Cerevisiae ◽  
Dolichyl Phosphate ◽  
Functional Homolog ◽  
Wide Range

In a wide range of organisms, dolichyl phosphate mannose (DPM) synthase is a complex of tree proteins Dpm1, Dpm2, and Dpm3. However, in the yeast Saccharomyces cerevisiae, it is believed to be a single Dpm1 protein. The function of Dpm3 is performed in S. cerevisiae by the C-terminal transmembrane domain of the catalytic subunit Dpm1. Until present, the regulatory Dpm2 protein has not been found in S. cerevisiae. In this study, we show that, in fact, the Yil102c-A protein interacts directly with Dpm1 in S. cerevisiae and influences its DPM synthase activity. Deletion of the YIL102c-A gene is lethal, and this phenotype is reversed by the dpm2 gene from Trichoderma reesei. Functional analysis of Yil102c-A revealed that it also interacts with glucosylphosphatidylinositol-N-acetylglucosaminyl transferase (GPI-GnT), similar to DPM2 in human cells. Taken together, these results show that Yil102c-A is a functional homolog of DPMII from T. reesei and DPM2 from humans.

scholarly journals Metabolic Engineering of Saccharomyces cerevisiae for Conversion of d-Glucose to Xylitol and Other Five-Carbon Sugars and Sugar Alcohols

2007 ◽  
Vol 73 (17) ◽  
pp. 5471-5476 ◽  
Author(s):  
Mervi H. Toivari ◽  
Laura Ruohonen ◽  
Andrei N. Miasnikov ◽  
Peter Richard ◽  
Merja Penttilä
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Metabolic Engineering ◽  
Growth Medium ◽  
Fold Increase ◽  
Pichia Stipitis ◽  
Xylitol Dehydrogenase ◽  
Sugar Alcohols ◽  
Pentose Sugar ◽  
Encoding Gene ◽  
Pentose Sugars

ABSTRACT Recombinant Saccharomyces cerevisiae strains that produce the sugar alcohols xylitol and ribitol and the pentose sugar d-ribose from d-glucose in a single fermentation step are described. A transketolase-deficient S. cerevisiae strain accumulated d-xylulose 5-phosphate intracellularly and released ribitol and pentose sugars (d-ribose, d-ribulose, and d-xylulose) into the growth medium. Expression of the xylitol dehydrogenase-encoding gene XYL2 of Pichia stipitis in the transketolase-deficient strain resulted in an 8.5-fold enhancement of the total amount of the excreted sugar alcohols ribitol and xylitol. The additional introduction of the 2-deoxy-glucose 6-phosphate phosphatase-encoding gene DOG1 into the transketolase-deficient strain expressing the XYL2 gene resulted in a further 1.6-fold increase in ribitol production. Finally, deletion of the endogenous xylulokinase-encoding gene XKS1 was necessary to increase the amount of xylitol to 50% of the 5-carbon sugar alcohols excreted.

Sign in / Sign up

Export Citation Format

Share Document