The mechanistic insight into the biomilling of goethite (α-FeO(OH)) nanorods using the yeast Saccharomyces cerevisiae

RSC Advances ◽  
2015 ◽  
Vol 5 (111) ◽  
pp. 91785-91794 ◽  
Author(s):  
Chandrashekhar Sharan ◽  
Puneet Khandelwal ◽  
Pankaj Poddar
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Complexes ◽  
Surface Form ◽  
Yeast Saccharomyces Cerevisiae ◽  
Mechanistic Insight ◽  
P Proteins ◽  
Insight Into

Proteins react with the Fe3+ ions on goethite surface, form Fe3+–protein complexes which get disassociated, and results into fresh Fe3+ ions on the surface. This process of complexation–dissociation leads to biomilling.

Measurements of intracellularATP provide new insight into the regulation of glycolysis in the yeast Saccharomyces cerevisiae

2012 ◽  
Vol 4 (1) ◽  
pp. 99-107 ◽  
Author(s):  
Cecilie K. Ytting ◽  
Anja T. Fuglsang ◽  
J. Kalervo Hiltunen ◽  
Alexander J. Kastaniotis ◽  
Veli Cengiz Özalp ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Yeast Saccharomyces Cerevisiae ◽  
Regulation Of Glycolysis ◽  
Insight Into

scholarly journals The Identification of Transposon-Tagged Mutations in Essential Genes That Affect Cell Morphology in Saccharomyces cerevisiae

Genetics ◽  
1996 ◽  
Vol 142 (1) ◽  
pp. 39-50 ◽  
Author(s):  
Kristin T Chun ◽  
Mark G Goebl
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Large Collection ◽  
Yeast Saccharomyces Cerevisiae ◽  
Bud Formation ◽  
Bud Development ◽  
Comprehensive Collection ◽  
Terminal Bud ◽  
Mutant Phenotypes ◽  
Insight Into ◽  
Bud Morphology

The yeast Saccharomyces cerevisiae reproduces by budding, and many genes are required for proper bud development. Mutations in some of these genes cause cells to die with an unusual terminal morphology—elongated or otherwise aberrantly shaped buds. To gain insight into bud development, we set out to identify novel genes that encode proteins required for proper bud morphogenesis. Previous studies screened collections of conditional mutations to identify genes required for essential functions, including bud formation. However, genes that are not susceptible to the generation of mutations that cause a conditional phenotype will not be identified in such screens. To identify a more comprehensive collection of mutants, we used transposon mutagenesis to generate a large collection of lethal disruption mutations. This collection was used to identify 209 mutants with disruptions that cause an aberrant terminal bud morphology. The disruption mutations in 33 of these mutants identify three previously uncharacterized genes as essential, and the mutant phenotypes suggest roles for their products in bud morphogenesis.

scholarly journals Mitochondrial Genomic Dysfunction Causes Dephosphorylation of Sch9 in the Yeast Saccharomyces cerevisiae

2011 ◽  
Vol 10 (10) ◽  
pp. 1367-1369 ◽  
Author(s):  
Shigeyuki Kawai ◽  
Jörg Urban ◽  
Manuele Piccolis ◽  
Nicolas Panchaud ◽  
Claudio De Virgilio ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Mechanisms ◽  
Retrograde Signaling ◽  
Yeast Saccharomyces Cerevisiae ◽  
Content Type ◽  
Insight Into

ABSTRACTTORC1-dependent phosphorylation ofSaccharomyces cerevisiaeSch9 was dramatically reduced upon exposure to a protonophore or in respiration-incompetent ρ0cells but not in respiration-incompetentpetmutants, providing important insight into the molecular mechanisms governing interorganellar signaling in general and retrograde signaling in particular.

scholarly journals A novel 66-kilodalton protein complexes with Rrn6, Rrn7, and TATA-binding protein to promote polymerase I transcription initiation in Saccharomyces cerevisiae.

1996 ◽  
Vol 16 (11) ◽  
pp. 6436-6443 ◽  
Author(s):  
C W Lin ◽  
B Moorefield ◽  
J Payne ◽  
P Aprikian ◽  
K Mitomo ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcription Initiation ◽  
Protein Complexes ◽  
Binding Protein ◽  
Strong Association ◽  
Tata Binding Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Pol I ◽  
Polymerase I

We report the cloning of RRN11, a gene coding for a 66-kDa protein essential for transcription initiation by RNA polymerase I (Pol I) in the yeast Saccharomyces cerevisiae. Rrn11 specifically complexes with two previously identified transcription factors, Rrn6 and Rrn7 (D. A. Keys, J. S. Steffan, J. A. Dodd, R. T. Yamamoto, Y. Nogi, and M. Nomura, Genes Dev. 8:2349-2362, 1994). The Rrn11-Rrn6-Rrn7 complex also binds the TATA-binding protein and is required for transcription by the core domain of the Pol I promoter. Therefore, we have designated the Rrn11-Rrn6-Rrn7-TATA-binding protein complex the yeast Pol I core factor. A two-hybrid assay was used to demonstrate involvement of short leucine heptad repeats on both Rrn11 and Rrn6 in the in vivo association of these two proteins. This assay also verified the previously described strong association between Rrn6 and Rrn7, independent of the Rrn6 leucine repeat.

Global landscape of protein complexes in the yeast Saccharomyces cerevisiae

Nature ◽  
2006 ◽  
Vol 440 (7084) ◽  
pp. 637-643 ◽  
Author(s):  
Nevan J. Krogan ◽  
Gerard Cagney ◽  
Haiyuan Yu ◽  
Gouqing Zhong ◽  
Xinghua Guo ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Complexes ◽  
Yeast Saccharomyces Cerevisiae

scholarly journals A Bir1p–Sli15p Kinetochore Passenger Complex Regulates Septin Organization during Anaphase

2007 ◽  
Vol 18 (10) ◽  
pp. 3820-3834 ◽  
Author(s):  
Scott Thomas ◽  
Kenneth B. Kaplan
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Recent Work ◽  
Protein Complexes ◽  
Critical Role ◽  
Aurora B ◽  
Yeast Saccharomyces Cerevisiae ◽  
Binding Factor ◽  
Complex Functions ◽  
Passenger Protein ◽  
Segregation Of Chromosomes

Kinetochore–passenger complexes in metazoans have been proposed to coordinate the segregation of chromosomes in anaphase with the induction of cytokinesis. Passenger protein homologues in the budding yeast Saccharomyces cerevisiae play a critical role early in mitosis, ensuring proper biorientation of kinetochore–microtubule attachments. Our recent work has implicated the passenger protein Bir1p (Survivin) and the inner kinetochore complex centromere binding factor 3 (CBF3) in the regulation of septin dynamics during anaphase. Here, we present data that is consistent with there being multiple passenger protein complexes. Our data show that Bir1p links together a large passenger complex containing Ndc10p, Sli15p (INCENP), and Ipl1p (Aurora B) and that the interaction between Bir1p and Sli15p is specifically involved in regulating septin dynamics during anaphase. Neither conditional alleles nor mutants of BIR1 that disrupt the interaction between Bir1p and Sli15p resulted in mono-attached kinetochores, suggesting that the Bir1p–Sli15p complex functions in anaphase and independently from Sli15p–Ipl1p complexes. We present a model for how discrete passenger complexes coordinate distinct aspects of mitosis.

Proteomic analysis of chromatin-modifying complexes in Saccharomyces cerevisiae identifies novel subunits

2004 ◽  
Vol 32 (6) ◽  
pp. 899-903 ◽  
Author(s):  
K.K. Lee ◽  
P. Prochasson ◽  
L. Florens ◽  
S.K. Swanson ◽  
M.P. Washburn ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Identification ◽  
Protein Complexes ◽  
Affinity Purification ◽  
Large Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Chromatin Remodelling Complex ◽  
Novel Proteins ◽  
Multidimensional Protein Identification Technology ◽  
Covalent Histone Modifications

Epigenetics is the alteration of phenotype without affecting the genotype. An underlying molecular mechanism of epigenetics is the changes of chromatin structure by covalent histone modifications and nucleosome reorganization. In the yeast, Saccharomyces cerevisiae, two of the most well-studied macromolecular complexes that perform these epigenetic changes are the ATP-dependent Swi/Snf chromatin-remodelling complex and the SAGA histone acetyltransferase complex. To understand fully the mechanism by which these large protein complexes perform their functions in the cell, it is crucial that all the subunits of these complexes are identified. In an attempt to identify new subunits associated with SAGA and Swi/Snf, we used tandem affinity purification, followed by a multidimensional protein identification technology to analyse the subunit composition. Our analysis identified two novel proteins, one associated with SAGA, YPL047W (Sgf11), and another associated with Swi/Snf, Rtt102.

A Unique Class of Conditional sir2 Mutants Displays Distinct Silencing Defects in Saccharomyces cerevisiae

Genetics ◽  
2002 ◽  
Vol 162 (2) ◽  
pp. 721-736 ◽  
Author(s):  
Sandra N Garcia ◽  
Lorraine Pillus
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Catalytic Activity ◽  
Dna Binding Domain ◽  
Catalytic Core ◽  
Conserved Residues ◽  
Mutant Proteins ◽  
Mechanistic Insight ◽  
Chromatin Proteins ◽  
Insight Into ◽  
Subtelomeric Regions

Abstract Silencing provides a critical means of repressing transcription through the assembly and modification of chromatin proteins. The NAD+-dependent deacetylation of histones by the Sir2p family of proteins lends mechanistic insight into how SIR2 contributes to silencing. Here we describe three locus-specific sir2 mutants that have a spectrum of silencing phenotypes in yeast. These mutants are dependent on SIR1 for silencing function at the HM silent mating-type loci, display distinct phenotypes at the rDNA, and have dominant silencing defects at the telomeres. Telomeric silencing is restored if the mutant proteins are directly tethered to subtelomeric regions, via a Gal4p DNA-binding domain (GBD), or are recruited by tethered GBD-Sir1p. These sir2 mutations are found within conserved residues of the SIR2 family and lead to defects in catalytic activity. Since one of the mutations lies outside the previously defined minimal catalytic core, our results show that additional regions of Sir2p can be important for enzymatic activity and that differences in levels of activity may have distinct effects at the silenced loci.

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