scholarly journals The AMPK Family Member Snf1 Protects Saccharomyces cerevisiae Cells upon Glutathione Oxidation

PLoS ONE ◽  
2013 ◽  
Vol 8 (3) ◽  
pp. e58283 ◽  
Author(s):  
Maria Pérez-Sampietro ◽  
Celia Casas ◽  
Enrique Herrero
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Family Member ◽  
Glutathione Oxidation

scholarly journals Capped mRNA Degradation Intermediates Accumulate in the Yeast spb8-2 Mutant

1998 ◽  
Vol 18 (9) ◽  
pp. 5062-5072 ◽  
Author(s):  
Ronald Boeck ◽  
Bruno Lapeyre ◽  
Christine E. Brown ◽  
Alan B. Sachs
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Family Member ◽  
Gene Deletion ◽  
Binding Protein ◽  
Mrna Degradation ◽  
Protein Family ◽  
Suppressor Mutation ◽  
Mrna Decapping ◽  
Mrna Species ◽  
Degradation Intermediates

ABSTRACT mRNA in the yeast Saccharomyces cerevisiae is primarily degraded through a pathway that is stimulated by removal of the mRNA cap structure. Here we report that a mutation in the SPB8(YJL124c) gene, initially identified as a suppressor mutation of a poly(A)-binding protein (PAB1) gene deletion, stabilizes the mRNA cap structure. Specifically, we find that thespb8-2 mutation results in the accumulation of capped, poly(A)-deficient mRNAs. The presence of this mutation also allows for the detection of mRNA species trimmed from the 3′ end. These data show that this Sm-like protein family member is involved in the process of mRNA decapping, and they provide an example of 3′-5′ mRNA degradation intermediates in yeast.

scholarly journals Molecular mechanisms of microtubule-dependent kinetochore transport toward spindle poles

2007 ◽  
Vol 178 (2) ◽  
pp. 269-281 ◽  
Author(s):  
Kozo Tanaka ◽  
Etsushi Kitamura ◽  
Yoko Kitamura ◽  
Tomoyuki U. Tanaka
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Family Member ◽  
Lateral Surface ◽  
Molecular Mechanisms ◽  
Microtubule Depolymerization ◽  
Spindle Poles ◽  
Dam1 Complex ◽  
Pulling Force

In mitosis, kinetochores are initially captured by the lateral sides of single microtubules and are subsequently transported toward spindle poles. Mechanisms for kinetochore transport are not yet known. We present two mechanisms involved in microtubule-dependent poleward kinetochore transport in Saccharomyces cerevisiae. First, kinetochores slide along the microtubule lateral surface, which is mainly and probably exclusively driven by Kar3, a kinesin-14 family member that localizes at kinetochores. Second, kinetochores are tethered at the microtubule distal ends and pulled poleward as microtubules shrink (end-on pulling). Kinetochore sliding is often converted to end-on pulling, enabling more processive transport, but the opposite conversion is rare. The establishment of end-on pulling is partly hindered by Kar3, and its progression requires the Dam1 complex. We suggest that the Dam1 complexes, which probably encircle a single microtubule, can convert microtubule depolymerization into the poleward kinetochore-pulling force. Thus, microtubule-dependent poleward kinetochore transport is ensured by at least two distinct mechanisms.

scholarly journals Testing for DNA Tracking by MOT1, a SNF2/SWI2 Protein Family Member

1999 ◽  
Vol 19 (1) ◽  
pp. 412-423 ◽  
Author(s):  
David T. Auble ◽  
Susanne M. Steggerda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcription Factor ◽  
Family Member ◽  
Binding Sites ◽  
Atp Hydrolysis ◽  
Tata Binding Protein ◽  
Protein Family ◽  
Dna Complexes ◽  
Dna Templates ◽  
Dependent Interaction

ABSTRACT Proteins in the SNF2/SWI2 family use ATP hydrolysis to catalyze rearrangements in diverse protein-DNA complexes. How ATP hydrolysis is coupled to these rearrangements is unknown, however. One attractive model is that these ATPases are ATP-dependent DNA-tracking enzymes. This idea was tested for the SNF2/SWI2 protein family member MOT1. MOT1 is an essential Saccharomyces cerevisiae transcription factor that uses ATP to dissociate TATA binding protein (TBP) from DNA. By using a series of DNA templates with one or two TATA boxes in combination with binding sites for heterologous DNA binding “roadblock” proteins, the ability of MOT1 to track along DNA was assayed. The results demonstrate that, following ATP-dependent TBP-DNA dissociation, MOT1 dissociates rapidly from the DNA by a mechanism that does not require a DNA end. Template commitment footprinting experiments support the conclusion that ATP-dependent DNA tracking by MOT1 does not occur. These results support a model in which MOT1 drives TBP-DNA dissociation by a mechanism that involves a transient, ATP-dependent interaction with TBP-DNA which does not involve ATP-dependent DNA tracking.

Feedback regulation of map kinase signal pathways

1996 ◽  
Vol 351 (1336) ◽  
pp. 143-149 ◽  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Family Member ◽  
Feedback Regulation ◽  
Signal Pathways ◽  
Phosphorylation Sites ◽  
Mapk Activation ◽  
Feedback Mechanisms ◽  
Mating Response ◽  
Erk Kinase

Ste7 is a MEK (MAPK /ERK kinase) family member that functions in the pheromone induced mating response pathway of Saccharomyces cerevisiae . We analysed the catalytic competence and in vivo function of Ste7 variants that have alterations of stimulatory and feedback phosphorylation sites. These analyses led us to unanticipated insights into two separate feedback mechanisms that impede the output of the mating response MAPK activation pathway.

scholarly journals The Sec1/Munc18 Protein, Vps33p, Functions at the Endosome and the Vacuole of Saccharomyces cerevisiae

2004 ◽  
Vol 15 (6) ◽  
pp. 2593-2605 ◽  
Author(s):  
Shoba Subramanian ◽  
Carol A. Woolford ◽  
Elizabeth W. Jones
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Family Member ◽  
Vesicle Fusion ◽  
Vacuolar Membrane ◽  
Late Endosome ◽  
Fusion Reactions ◽  
Sm Proteins ◽  
First Report ◽  
Sm Protein

The Sec1/Munc18 (SM) family of proteins is thought to impart compartmental specificity to vesicle fusion reactions. Here we report characterization of Vps33p, an SM family member previously thought to act exclusively at the vacuolar membrane with the vacuolar syntaxin Vam3p. Vacuolar morphology of vps33Δ cells resembles that of cells lacking both Vam3p and the endosomal syntaxin Pep12p, suggesting that Vps33p may function with these syntaxins at the vacuole and the endosome. Consistent with this, vps33 mutants secrete the Golgi precursor form of the vacuolar hydrolase CPY into the medium. We also demonstrate that Vps33p acts at other steps, for vps33 mutants show severe defects in endocytosis at the late endosome. At the endosome, Vps33p and other class C members exist as a complex with Vps8p, a protein previously known to act in transport between the late Golgi and the endosome. Vps33p also interacts with Pep12p, a known interactor of the SM protein Vps45p. High copy PEP7/VAC1 suppresses vacuolar morphology defects of vps33 mutants. These findings demonstrate that Vps33p functions at multiple trafficking steps and is not limited to action at the vacuolar membrane. This is the first report demonstrating the involvement of a single syntaxin with two SM proteins at the same organelle.

scholarly journals Structure of SWI/SNF chromatin remodeller RSC bound to a nucleosome

2019 ◽  
Author(s):  
Felix R. Wagner ◽  
Christian Dienemann ◽  
Haibo Wang ◽  
Alexandra Stützer ◽  
Dimitry Tegunov ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Family Member ◽  
Chromatin Remodelling ◽  
Family Function ◽  
Histone Octamer ◽  
Nucleosomal Dna ◽  
Cancer Mutations ◽  
Key Features ◽  
Protein Modules ◽  
Eukaryote Genome

AbstractChromatin remodelling complexes of the SWI/SNF family function in the formation of nucleosome-depleted regions and transcriptionally active promoters in the eukaryote genome. The structure of the Saccharomyces cerevisiae SWI/SNF family member RSC in complex with a nucleosome substrate reveals five protein modules and suggests key features of the remodelling mechanism. A DNA-interacting module grasps extra-nucleosomal DNA and helps to recruit RSC to promoters. The ATPase and arm modules sandwich the nucleosome disc with their ‘SnAC’ and ‘finger’ elements, respectively. The translocase motor engages with the edge of the nucleosome at superhelical location +2 to pump DNA along the nucleosome, resulting in a sliding of the histone octamer along DNA. The results elucidate how nucleosome-depleted regions are formed and provide a basis for understanding human chromatin remodelling complexes of the SWI/SNF family and the consequences of cancer mutations that frequently occur in these complexes.

scholarly journals The Fission Yeast Kinetochore Component Spc7 Associates with the EB1 Family Member Mal3 and Is Required for Kinetochore–Spindle Association

2004 ◽  
Vol 15 (12) ◽  
pp. 5255-5267 ◽  
Author(s):  
Anne Kerres ◽  
Corina Vietmeier-Decker ◽  
Jennifer Ortiz ◽  
Inga Karig ◽  
Christoph Beuter ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Saccharomyces Cerevisiae ◽  
Fission Yeast ◽  
Family Member ◽  
Binding Proteins ◽  
Centromere Region ◽  
Critical Aspect ◽  
Ndc80 Complex ◽  
Mutant Strains ◽  
Spindle Microtubules

A critical aspect of mitosis is the interaction of the kinetochore with spindle microtubules. Fission yeast Mal3 is a member of the EB1 family of microtubule plus-end binding proteins, which have been implicated in this process. However, the Mal3 interaction partner at the kinetochore had not been identified. Here, we show that the mal3 mutant phenotype can be suppressed by the presence of extra Spc7, an essential kinetochore protein associated with the central centromere region. Mal3 and Spc7 interact physically as both proteins can be coimmunoprecipitated. Overexpression of a Spc7 variant severely compromises kinetochore–microtubule interaction, indicating that the Spc7 protein plays a role in this process. Spc7 function seems to be conserved because, Spc105, a Saccharomyces cerevisiae homolog of Spc7, identified by mass spectrometry as a component of the conserved Ndc80 complex, can rescue mal3 mutant strains.

scholarly journals Stu2p, the budding yeast member of the conserved Dis1/XMAP215 family of microtubule-associated proteins is a plus end–binding microtubule destabilizer

2003 ◽  
Vol 161 (2) ◽  
pp. 359-369 ◽  
Author(s):  
Mark van Breugel ◽  
David Drechsel ◽  
Anthony Hyman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Division ◽  
Quantitative Analysis ◽  
Family Member ◽  
Budding Yeast ◽  
Microtubule Dynamics ◽  
Biochemical Activity ◽  
Microtubule Associated Proteins ◽  
Associated Proteins

The Dis1/XMAP215 family of microtubule-associated proteins conserved from yeast to mammals is essential for cell division. XMAP215, the Xenopus member of this family, has been shown to stabilize microtubules in vitro, but other members of this family have not been biochemically characterized. Here we investigate the properties of the Saccharomyces cerevisiae homologue Stu2p in vitro. Surprisingly, Stu2p is a microtubule destabilizer that binds preferentially to microtubule plus ends. Quantitative analysis of microtubule dynamics suggests that Stu2p induces microtubule catastrophes by sterically interfering with tubulin addition to microtubule ends. These results reveal both a new biochemical activity for a Dis1/XMAP215 family member and a novel mechanism for microtubule destabilization.

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