Faculty Opinions recommendation of Multimeric threading-based prediction of protein-protein interactions on a genomic scale: application to the Saccharomyces cerevisiae proteome.

2003 ◽  
Author(s):  
Rob Russell
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Genomic Scale

GRR1 of Saccharomyces cerevisiae is required for glucose repression and encodes a protein with leucine-rich repeats

1991 ◽  
Vol 11 (10) ◽  
pp. 5101-5112
Author(s):  
J S Flick ◽  
M Johnston
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Interactions ◽  
Tandem Repeats ◽  
Glucose Repression ◽  
Molecular Data ◽  
Primary Response ◽  
Yeast Cells ◽  
Cell Fractionation ◽  
Protein Protein Interactions ◽  
Yeast Saccharomyces Cerevisiae

Growth of the yeast Saccharomyces cerevisiae on glucose leads to repression of transcription of many genes required for alternative carbohydrate metabolism. The GRR1 gene appears to be of central importance to the glucose repression mechanism, because mutations in GRR1 result in a pleiotropic loss of glucose repression (R. Bailey and A. Woodword, Mol. Gen. Genet. 193:507-512, 1984). We have isolated the GRR1 gene and determined that null mutants are viable and display a number of growth defects in addition to the loss of glucose repression. Surprisingly, grr1 mutations convert SUC2, normally a glucose-repressed gene, into a glucose-induced gene. GRR1 encodes a protein of 1,151 amino acids that is expressed constitutively at low levels in yeast cells. GRR1 protein contains 12 tandem repeats of a sequence similar to leucine-rich motifs found in other proteins that may mediate protein-protein interactions. Indeed, cell fractionation studies are consistent with this view, suggesting that GRR1 protein is tightly associated with a particulate protein fraction in yeast extracts. The combined genetic and molecular data are consistent with the idea that GRR1 protein is a primary response element in the glucose repression pathway and is required for the generation or interpretation of the signal that induces glucose repression.

scholarly journals Saccharomyces cerevisiae as a Tool to Investigate Plant Potassium and Sodium Transporters

2019 ◽  
Vol 20 (9) ◽  
pp. 2133 ◽  
Author(s):  
Antonella Locascio ◽  
Nuria Andrés-Colás ◽  
José Miguel Mulet ◽  
Lynne Yenush
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Interactions ◽  
Model System ◽  
Protein Protein Interactions ◽  
Alkali Cations ◽  
Yeast Saccharomyces Cerevisiae ◽  
Future Directions ◽  
Sodium Transporters ◽  
Adverse Environmental Conditions ◽  
Sodium And Potassium

Sodium and potassium are two alkali cations abundant in the biosphere. Potassium is essential for plants and its concentration must be maintained at approximately 150 mM in the plant cell cytoplasm including under circumstances where its concentration is much lower in soil. On the other hand, sodium must be extruded from the plant or accumulated either in the vacuole or in specific plant structures. Maintaining a high intracellular K+/Na+ ratio under adverse environmental conditions or in the presence of salt is essential to maintain cellular homeostasis and to avoid toxicity. The baker’s yeast, Saccharomyces cerevisiae, has been used to identify and characterize participants in potassium and sodium homeostasis in plants for many years. Its utility resides in the fact that the electric gradient across the membrane and the vacuoles is similar to plants. Most plant proteins can be expressed in yeast and are functional in this unicellular model system, which allows for productive structure-function studies for ion transporting proteins. Moreover, yeast can also be used as a high-throughput platform for the identification of genes that confer stress tolerance and for the study of protein–protein interactions. In this review, we summarize advances regarding potassium and sodium transport that have been discovered using the yeast model system, the state-of-the-art of the available techniques and the future directions and opportunities in this field.

scholarly journals Novel Role for the C Terminus of Saccharomyces cerevisiae Rev1 in Mediating Protein-Protein Interactions

2006 ◽  
Vol 26 (21) ◽  
pp. 8173-8182 ◽  
Author(s):  
Sanjay D'Souza ◽  
Graham C. Walker
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Damage ◽  
Protein Interactions ◽  
Sequence Similarity ◽  
Dna Lesions ◽  
Dominant Negative ◽  
Dominant Negative Effect ◽  
Protein Protein Interactions ◽  
C Terminus ◽  
Negative Effect

ABSTRACT The Saccharomyces cerevisiae REV3/7-encoded polymerase ζ and Rev1 are central to the replicative bypass of DNA lesions, a process called translesion synthesis (TLS). While yeast polymerase ζ extends from distorted DNA structures, Rev1 predominantly incorporates C residues from across a template G and a variety of DNA lesions. Intriguingly, Rev1 catalytic activity does not appear to be required for TLS. Instead, yeast Rev1 is thought to participate in TLS by facilitating protein-protein interactions via an N-terminal BRCT motif. In addition, higher eukaryotic homologs of Rev1 possess a C terminus that interacts with other TLS polymerases. Due to a lack of sequence similarity, the yeast Rev1 C-terminal region, located after the polymerase domain, had initially been thought not to play a role in TLS. Here, we report that elevated levels of the yeast Rev1 C terminus confer a strong dominant-negative effect on viability and induced mutagenesis after DNA damage, highlighting the crucial role that the C terminus plays in DNA damage tolerance. We show that this phenotype requires REV7 and, using immunoprecipitations from crude extracts, demonstrate that, in addition to the polymerase-associated domain, the extreme Rev1 C terminus and the BRCT region of Rev1 mediate interactions with Rev7.

scholarly journals GRR1 of Saccharomyces cerevisiae is required for glucose repression and encodes a protein with leucine-rich repeats.

1991 ◽  
Vol 11 (10) ◽  
pp. 5101-5112 ◽  
Author(s):  
J S Flick ◽  
M Johnston
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Interactions ◽  
Tandem Repeats ◽  
Glucose Repression ◽  
Molecular Data ◽  
Primary Response ◽  
Yeast Cells ◽  
Cell Fractionation ◽  
Protein Protein Interactions ◽  
Yeast Saccharomyces Cerevisiae

Growth of the yeast Saccharomyces cerevisiae on glucose leads to repression of transcription of many genes required for alternative carbohydrate metabolism. The GRR1 gene appears to be of central importance to the glucose repression mechanism, because mutations in GRR1 result in a pleiotropic loss of glucose repression (R. Bailey and A. Woodword, Mol. Gen. Genet. 193:507-512, 1984). We have isolated the GRR1 gene and determined that null mutants are viable and display a number of growth defects in addition to the loss of glucose repression. Surprisingly, grr1 mutations convert SUC2, normally a glucose-repressed gene, into a glucose-induced gene. GRR1 encodes a protein of 1,151 amino acids that is expressed constitutively at low levels in yeast cells. GRR1 protein contains 12 tandem repeats of a sequence similar to leucine-rich motifs found in other proteins that may mediate protein-protein interactions. Indeed, cell fractionation studies are consistent with this view, suggesting that GRR1 protein is tightly associated with a particulate protein fraction in yeast extracts. The combined genetic and molecular data are consistent with the idea that GRR1 protein is a primary response element in the glucose repression pathway and is required for the generation or interpretation of the signal that induces glucose repression.

A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae

Nature ◽  
2000 ◽  
Vol 403 (6770) ◽  
pp. 623-627 ◽  
Author(s):  
Peter Uetz ◽  
Loic Giot ◽  
Gerard Cagney ◽  
Traci A. Mansfield ◽  
Richard S. Judson ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Interactions ◽  
Comprehensive Analysis ◽  
Protein Protein Interactions

scholarly journals Interactions of Sen1, Nrd1, and Nab3 with Multiple Phosphorylated Forms of the Rpb1 C-Terminal Domain in Saccharomyces cerevisiae

2012 ◽  
Vol 11 (4) ◽  
pp. 417-429 ◽  
Author(s):  
Karen Chinchilla ◽  
Juan B. Rodriguez-Molina ◽  
Doris Ursic ◽  
Jonathan S. Finkel ◽  
Aseem Z. Ansari ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Polymerase Ii ◽  
Protein Interactions ◽  
Noncoding Rna ◽  
Protein Protein Interactions ◽  
Coding Region ◽  
Protein Coding ◽  
Content Type ◽  
Protein Coding Genes ◽  
Terminal Domain

ABSTRACT The Saccharomyces cerevisiae SEN1 gene codes for a nuclear, ATP-dependent helicase which is embedded in a complex network of protein-protein interactions. Pleiotropic phenotypes of mutations in SEN1 suggest that Sen1 functions in many nuclear processes, including transcription termination, DNA repair, and RNA processing. Sen1, along with termination factors Nrd1 and Nab3, is required for the termination of noncoding RNA transcripts, but Sen1 is associated during transcription with coding and noncoding genes. Sen1 and Nrd1 both interact directly with Nab3, as well as with the C-terminal domain (CTD) of Rpb1, the largest subunit of RNA polymerase II. It has been proposed that Sen1, Nab3, and Nrd1 form a complex that associates with Rpb1 through an interaction between Nrd1 and the Ser 5 -phosphorylated (Ser 5 -P) CTD. To further study the relationship between the termination factors and Rpb1, we used two-hybrid analysis and immunoprecipitation to characterize sen1-R302W , a mutation that impairs an interaction between Sen1 and the Ser 2 -phosphorylated CTD. Chromatin immunoprecipitation indicates that the impairment of the interaction between Sen1 and Ser 2 -P causes the reduced occupancy of mutant Sen1 across the entire length of noncoding genes. For protein-coding genes, mutant Sen1 occupancy is reduced early and late in transcription but is similar to that of the wild type across most of the coding region. The combined data suggest a handoff model in which proteins differentially transfer from the Ser 5 - to the Ser 2 -phosphorylated CTD to promote the termination of noncoding transcripts or other cotranscriptional events for protein-coding genes.

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