scholarly journals Functional analysis of the global repressor Tup1 for maltose metabolism in Saccharomyces cerevisiae: different roles of the functional domains

2017 ◽  
Vol 16 (1) ◽  
Author(s):  
Xue Lin ◽  
Ai-Qun Yu ◽  
Cui-Ying Zhang ◽  
Li Pi ◽  
Xiao-Wen Bai ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Functional Analysis ◽  
Functional Domains ◽  
Maltose Metabolism

The HML mating-type cassette of Saccharomyces cerevisiae is regulated by two separate but functionally equivalent silencers

1989 ◽  
Vol 9 (11) ◽  
pp. 4621-4630
Author(s):  
D J Mahoney ◽  
J R Broach
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mating Type ◽  
Binding Sites ◽  
The Other ◽  
Functional Domains ◽  
Gene Products ◽  
Cis Acting ◽  
Full Expression ◽  
Mating Type Genes ◽  
Chromosome Iii

Mating-type genes resident in the silent cassette HML at the left arm of chromosome III are repressed by the action of four SIR gene products, most likely mediated through two cis-acting sites located on opposite sides of the locus. We showed that deletion of either of these two cis-acting sites from the chromosome did not yield any detectable derepression of HML, while deletion of both sites yielded full expression of the locus. In addition, each of these sites was capable of exerting repression of heterologous genes inserted in their vicinity. Thus, HML expression is regulated by two independent silencers, each fully competent for maintaining repression. This situation was distinct from the organization of the other silent locus, HMR, at which a single silencer served as the predominant repressor of expression. Examination of identifiable domains and binding sites within the HML silencers suggested that silencing activity can be achieved by a variety of combinations of various functional domains.

Screening for Theileria parva secretory gene products by functional analysis in Saccharomyces cerevisiae

2000 ◽  
Vol 109 (1) ◽  
pp. 81-87 ◽  
Author(s):  
Susan Musembi ◽  
Rozmin Janoo ◽  
Bali Sohanpal ◽  
Horace Ochanda ◽  
Onesmo ole-MoiYoi ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Functional Analysis ◽  
Gene Products ◽  
Theileria Parva

scholarly journals Functional analysis of human aromatic amino acid transporter MCT10/TAT1 using the yeast Saccharomyces cerevisiae

2017 ◽  
Vol 1859 (10) ◽  
pp. 2076-2085 ◽  
Author(s):  
Satoshi Uemura ◽  
Takahiro Mochizuki ◽  
Goyu Kurosaka ◽  
Takanori Hashimoto ◽  
Yuki Masukawa ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Functional Analysis ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Amino Acid Transporter ◽  
Yeast Saccharomyces Cerevisiae ◽  
Acid Transporter

scholarly journals Analysis of functional domains of Wilson disease protein (ATP7B) in Saccharomyces cerevisiae

FEBS Letters ◽  
1998 ◽  
Vol 428 (3) ◽  
pp. 281-285 ◽  
Author(s):  
Masatake Iida ◽  
Kunihiko Terada ◽  
Yoshihiro Sambongi ◽  
Tokumitsu Wakabayashi ◽  
Naoyuki Miura ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Wilson Disease ◽  
Functional Domains ◽  
Wilson Disease Protein ◽  
Disease Protein

Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae

1990 ◽  
Vol 10 (5) ◽  
pp. 2224-2236
Author(s):  
N Ogawa ◽  
Y Oshima
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcriptional Activation ◽  
Transcriptional Control ◽  
Regulatory Protein ◽  
Mitochondrial Protein ◽  
Functional Domains ◽  
Regulatory Factor ◽  
Coding Region ◽  
Protein Determination ◽  
Transcriptional Activation Domain

The PHO4 gene encodes a positive regulatory factor involved in regulating transcription of various genes in the phosphatase regulon of Saccharomyces cerevisiae. Besides its own coding region, the 1.8-kilobase PHO4 transcript contains a coding region for a mitochondrial protein which does not appear to be translated. Four functional domains were found in the PHO4 protein, which consists of 312 amino acid (aa) residues as deduced from the open reading frame of PHO4. A gel retardation assay with beta-galactosidase::PHO4 fused protein revealed that the 85-aa C terminus is the domain responsible for binding to the promoter DNA of PHO5, a gene under the control of PHO4. This region has similarities with the amphipathic helix-loop-helix motif of c-myc protein. Determination of the nucleotide sequences of four PHO4c mutant alleles and insertion and deletion analyses of PHO4 DNA indicated that a region from aa 163 to 202 is involved in interaction with a negative regulatory factor PHO80. Complementation of a pho4 null allele with the modified PHO4 DNAs suggested that the N-terminal region (1 to 109 aa), which is rich in acidic aa, is the transcriptional activation domain. The deleterious effects of various PHO4 mutations on the constitutive transcription of PHO5 in PHO4c mutant cells suggested that the region from aa 203 to 227 is involved in oligomerization of the PHO4 protein.

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 Evolutionary and Functional Analysis of the Invariant SWIM Domain in the Conserved Shu2/SWS1 Protein Family from Saccharomyces cerevisiae to Homo sapiens

Genetics ◽  
2015 ◽  
Vol 199 (4) ◽  
pp. 1023-1033 ◽  
Author(s):  
Stephen K. Godin ◽  
Camille Meslin ◽  
Faiz Kabbinavar ◽  
Dominique S. Bratton-Palmer ◽  
Christina Hornack ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Functional Analysis ◽  
Homo Sapiens ◽  
Protein Family
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