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Article: Pil1 cytoplasmic rods contain bundles of crosslinked tubules.

Kabeche, Ruth / Howard, Louisa / Moseley, James B

2015 Volume 8, Issue 1, Page(s) e990848

Abstract: Cytoskeletal polymers are organized into a wide variety of higher-order structures in cells. The yeast BAR domain protein Pil1 self-assembles into tubules in vitro, and forms linear polymers at cortical eisosomes in cells. In the fission yeast S. pombe, ... ...

Abstract	Cytoskeletal polymers are organized into a wide variety of higher-order structures in cells. The yeast BAR domain protein Pil1 self-assembles into tubules in vitro, and forms linear polymers at cortical eisosomes in cells. In the fission yeast S. pombe, over-expressed Pil1 forms thick rods that detach from the plasma membrane. In this study, we used thin-section electron microscopy to determine the ultrastructure of these cytoplasmic Pil1 rods. We found that cytoplasmic rods contained crosslinked Pil1 tubules that displayed regular, hexagonal spacing. These bundles were stained by filipin, a sterol-binding fluorescent dye, suggesting that they contained lipids. Cytoplasmic Pil1 rods were present but less abundant in sle1Δ and fhn1Δ mutant cells. We also found that endogenous Pil1 formed thick rods under saturated growth conditions. Taken together, our findings suggest the presence of cellular mechanisms that assemble Pil1 tubules into higher-order structures.
Language	English
Publishing date	2015-03-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	2451097-X
ISSN	1942-0889
ISSN	1942-0889
DOI	10.4161/19420889.2014.990848
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Article ; Online: Eisosomes provide membrane reservoirs for rapid expansion of the yeast plasma membrane.

Kabeche, Ruth / Howard, Louisa / Moseley, James B

Journal of cell science

2015 Volume 128, Issue 22, Page(s) 4057–4062

Abstract: Cell surface area rapidly increases during mechanical and hypoosmotic stresses. Such expansion of the plasma membrane requires 'membrane reservoirs' that provide surface area and buffer membrane tension, but the sources of this membrane remain poorly ... ...

Abstract	Cell surface area rapidly increases during mechanical and hypoosmotic stresses. Such expansion of the plasma membrane requires 'membrane reservoirs' that provide surface area and buffer membrane tension, but the sources of this membrane remain poorly understood. In principle, the flattening of invaginations and buds within the plasma membrane could provide this additional surface area, as recently shown for caveolae in animal cells. Here, we used microfluidics to study the rapid expansion of the yeast plasma membrane in protoplasts, which lack the rigid cell wall. To survive hypoosmotic stress, yeast cell protoplasts required eisosomes, protein-based structures that generate long invaginations at the plasma membrane. Both budding yeast and fission yeast protoplasts lacking eisosomes were unable to expand like wild-type protoplasts during hypoosmotic stress, and subsequently lysed. By performing quantitative fluorescence microscopy on single protoplasts, we also found that eisosomes disassembled as surface area increased. During this process, invaginations generated by eisosomes at the plasma membrane became flattened, as visualized by scanning electron microscopy. We propose that eisosomes serve as tension-dependent membrane reservoirs for expansion of yeast cells in an analogous manner to caveolae in animal cells.
MeSH term(s)	Animals ; Cell Membrane/metabolism ; Models, Biological ; Protoplasts/metabolism ; Yeasts/metabolism
Language	English
Publishing date	2015-11-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.176867
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Article ; Online: Eisosomes Regulate Phosphatidylinositol 4,5-Bisphosphate (PI(4,5)P2) Cortical Clusters and Mitogen-activated Protein (MAP) Kinase Signaling upon Osmotic Stress.

Kabeche, Ruth / Madrid, Marisa / Cansado, José / Moseley, James B

The Journal of biological chemistry

2015 Volume 290, Issue 43, Page(s) 25960–25973

Abstract: Eisosomes are multiprotein structures that generate linear invaginations at the plasma membrane of yeast cells. The core component of eisosomes, the BAR domain protein Pil1, generates these invaginations through direct binding to lipids including ... ...

Abstract	Eisosomes are multiprotein structures that generate linear invaginations at the plasma membrane of yeast cells. The core component of eisosomes, the BAR domain protein Pil1, generates these invaginations through direct binding to lipids including phosphoinositides. Eisosomes promote hydrolysis of phosphatidylinositol 4,5 bisphosphate (PI(4,5)P2) by functioning with synaptojanin, but the cellular processes regulated by this pathway have been unknown. Here, we found that PI(4,5)P2 regulation by eisosomes inhibits the cell integrity pathway, a conserved MAPK signal transduction cascade. This pathway is activated by multiple environmental conditions including osmotic stress in the fission yeast Schizosaccharomyces pombe. Activation of the MAPK Pmk1 was impaired by mutations in the phosphatidylinositol (PI) 5-kinase Its3, but this defect was suppressed by removal of eisosomes. Using fluorescent biosensors, we found that osmotic stress induced the formation of PI(4,5)P2 clusters that were spatially organized by eisosomes in both fission yeast and budding yeast cells. These cortical clusters contained the PI 5-kinase Its3 and did not assemble in the its3-1 mutant. The GTPase Rho2, an upstream activator of Pmk1, also co-localized with PI(4,5)P2 clusters under osmotic stress, providing a molecular link between these novel clusters and MAPK activation. Our findings have revealed that eisosomes regulate activation of MAPK signal transduction through the organization of cortical lipid-based microdomains.
MeSH term(s)	MAP Kinase Signaling System/physiology ; Organelles/physiology ; Osmotic Pressure ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Schizosaccharomyces/enzymology ; Schizosaccharomyces/metabolism
Chemical Substances	Phosphatidylinositol 4,5-Diphosphate
Language	English
Publishing date	2015-09-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M115.674192
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Article ; Online: A Pil1-Sle1-Syj1-Tax4 functional pathway links eisosomes with PI(4,5)P2 regulation.

Kabeche, Ruth / Roguev, Assen / Krogan, Nevan J / Moseley, James B

Journal of cell science

2014 Volume 127, Issue Pt 6, Page(s) 1318–1326

Abstract: Stable compartments of the plasma membrane promote a wide range of cellular functions. In yeast cells, cytosolic structures called eisosomes generate prominent cortical invaginations of unknown function. Through a series of genetic screens in fission ... ...

Abstract	Stable compartments of the plasma membrane promote a wide range of cellular functions. In yeast cells, cytosolic structures called eisosomes generate prominent cortical invaginations of unknown function. Through a series of genetic screens in fission yeast, we found that the eisosome proteins Pil1 and Sle1 function with the synaptojanin-like lipid phosphatase Syj1 and its ligand Tax4. This genetic pathway connects eisosome function with the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PI(4,5)P2] in cells. Defects in PI(4,5)P2 regulation led to eisosome defects, and we found that the core eisosome protein Pil1 can bind to and tubulate liposomes containing PI(4,5)P2. Mutations in components of the Pil1-Sle1-Syj1-Tax4 pathway suppress the growth and morphology defects of TORC2 mutants, indicating that eisosome-dependent regulation of PI(4,5)P2 feeds into signal transduction pathways. We propose that the geometry of membrane invaginations generates spatial and temporal signals for lipid-mediated signaling events in cells.
MeSH term(s)	Adaptor Proteins, Vesicular Transport/metabolism ; Cytoskeletal Proteins/metabolism ; Liposomes ; Mechanistic Target of Rapamycin Complex 2 ; Multiprotein Complexes/metabolism ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Protein Transport ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/metabolism ; Signal Transduction ; TOR Serine-Threonine Kinases/metabolism
Chemical Substances	Adaptor Proteins, Vesicular Transport ; Cytoskeletal Proteins ; Liposomes ; Multiprotein Complexes ; Phosphatidylinositol 4,5-Diphosphate ; Pil1 protein, S pombe ; Schizosaccharomyces pombe Proteins ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1)
Language	English
Publishing date	2014-01-16
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.143545
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Article ; Online: TRIM37 controls cancer-specific vulnerability to PLK4 inhibition.

Meitinger, Franz / Ohta, Midori / Lee, Kian-Yong / Watanabe, Sadanori / Davis, Robert L / Anzola, John V / Kabeche, Ruth / Jenkins, David A / Shiau, Andrew K / Desai, Arshad / Oegema, Karen

Nature

2020 Volume 585, Issue 7825, Page(s) 440–446

Abstract: Centrosomes catalyse the formation of microtubules needed to assemble the mitotic spindle ... ...

Abstract	Centrosomes catalyse the formation of microtubules needed to assemble the mitotic spindle apparatus
MeSH term(s)	Animals ; Breast Neoplasms/genetics ; Breast Neoplasms/metabolism ; Breast Neoplasms/pathology ; Cell Line, Tumor ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosomes, Human, Pair 17/genetics ; Female ; Humans ; Mice ; Mice, Inbred BALB C ; Microtubule-Organizing Center/drug effects ; Microtubule-Organizing Center/metabolism ; Mitosis/drug effects ; Mitosis/genetics ; Neoplasms/drug therapy ; Neoplasms/enzymology ; Neoplasms/metabolism ; Neoplasms/pathology ; Neuroblastoma/genetics ; Neuroblastoma/metabolism ; Neuroblastoma/pathology ; Protein Stability ; Protein-Serine-Threonine Kinases/antagonists & inhibitors ; Protein-Serine-Threonine Kinases/chemistry ; Protein-Serine-Threonine Kinases/metabolism ; Pyrimidines/pharmacology ; Pyrimidines/therapeutic use ; Spindle Apparatus/drug effects ; Spindle Apparatus/metabolism ; Sulfones/pharmacology ; Sulfones/therapeutic use ; Tripartite Motif Proteins/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination ; Xenograft Model Antitumor Assays
Chemical Substances	Cep192 protein, human ; Chromosomal Proteins, Non-Histone ; Pyrimidines ; Sulfones ; Tripartite Motif Proteins ; Ubiquitin ; centrinone ; TRIM37 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; PLK4 protein, human (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2020-09-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-020-2710-1
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Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Megadalton-node assembly by binding of Skb1 to the membrane anchor Slf1.

Deng, Lin / Kabeche, Ruth / Wang, Ning / Wu, Jian-Qiu / Moseley, James B

Molecular biology of the cell

2014 Volume 25, Issue 17, Page(s) 2660–2668

Abstract: The plasma membrane contains both dynamic and static microdomains. Given the growing appreciation of cortical microdomains in cell biology, it is important to determine the organizational principles that underlie assembly of compartmentalized structures ... ...

Abstract	The plasma membrane contains both dynamic and static microdomains. Given the growing appreciation of cortical microdomains in cell biology, it is important to determine the organizational principles that underlie assembly of compartmentalized structures at the plasma membrane. The fission yeast plasma membrane is highly compartmentalized by distinct sets of cortical nodes, which control signaling for cell cycle progression and cytokinesis. The mitotic inhibitor Skb1 localizes to a set of cortical nodes that provide spatial control over signaling for entry into mitosis. However, it has been unclear whether these nodes contain other proteins and how they might be organized and tethered to the plasma membrane. Here we show that Skb1 forms nodes by interacting with the novel protein Slf1, which is a limiting factor for node formation in cells. Using quantitative fluorescence microscopy and in vitro assays, we demonstrate that Skb1-Slf1 nodes are megadalton structures that are anchored to the membrane by a lipid-binding region in the Slf1 C-terminus. We propose a mechanism for higher-order node formation by Skb1 and Slf1, with implications for macromolecular assemblies in diverse cell types.
MeSH term(s)	Cell Membrane/metabolism ; Chromatography, Liquid ; Conserved Sequence ; Membrane Microdomains/metabolism ; Methyltransferases/chemistry ; Methyltransferases/metabolism ; Methyltransferases/physiology ; Microscopy, Fluorescence ; Models, Molecular ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism ; RNA-Binding Proteins/physiology ; Schizosaccharomyces/chemistry ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/metabolism ; Schizosaccharomyces pombe Proteins/physiology ; Tandem Mass Spectrometry
Chemical Substances	RNA-Binding Proteins ; SLF1 protein, S pombe ; Schizosaccharomyces pombe Proteins ; Skb1 protein, S pombe ; Methyltransferases (EC 2.1.1.-)
Language	English
Publishing date	2014-07-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E14-04-0896
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Article ; Online: The filament-forming protein Pil1 assembles linear eisosomes in fission yeast.

Kabeche, Ruth / Baldissard, Suzanne / Hammond, John / Howard, Louisa / Moseley, James B

Molecular biology of the cell

2011 Volume 22, Issue 21, Page(s) 4059–4067

Abstract: The cortical cytoskeleton mediates a range of cellular activities such as endocytosis, cell motility, and the maintenance of cell rigidity. Traditional polymers, including actin, microtubules, and septins, contribute to the cortical cytoskeleton, but ... ...

Abstract	The cortical cytoskeleton mediates a range of cellular activities such as endocytosis, cell motility, and the maintenance of cell rigidity. Traditional polymers, including actin, microtubules, and septins, contribute to the cortical cytoskeleton, but additional filament systems may also exist. In yeast cells, cortical structures called eisosomes generate specialized domains termed MCCs to cluster specific proteins at sites of membrane invaginations. Here we show that the core eisosome protein Pil1 forms linear cortical filaments in fission yeast cells and that purified Pil1 assembles into filaments in vitro. In cells, Pil1 cortical filaments are excluded from regions of cell growth and are independent of the actin and microtubule cytoskeletons. Pil1 filaments assemble slowly at the cell cortex and appear stable by time-lapse microscopy and fluorescence recovery after photobleaching. This stability does not require the cell wall, but Pil1 and the transmembrane protein Fhn1 colocalize and are interdependent for localization to cortical filaments. Increased Pil1 expression leads to cytoplasmic Pil1 rods that are stable and span the length of cylindrical fission yeast cells. We propose that Pil1 is a novel component of the yeast cytoskeleton, with implications for the role of filament assembly in the spatial organization of cells.
MeSH term(s)	Apraxia, Ideomotor ; Cell Division ; Cell Membrane Structures/metabolism ; Cell Polarity ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Cytoskeleton/metabolism ; Endocytosis ; Fluorescence Recovery After Photobleaching ; Green Fluorescent Proteins/chemistry ; Green Fluorescent Proteins/metabolism ; Protein Multimerization ; Protein Stability ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Time-Lapse Imaging
Chemical Substances	Cytoskeletal Proteins ; Pil1 protein, S pombe ; Pil2 protein, S pombe ; Recombinant Fusion Proteins ; Schizosaccharomyces pombe Proteins ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2011-09-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E11-07-0605
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Article ; Online: CAG Expansions Are Genetically Stable and Form Nontoxic Aggregates in Cells Lacking Endogenous Polyglutamine Proteins.

Zurawel, Ashley A / Kabeche, Ruth / DiGregorio, Sonja E / Deng, Lin / Menon, Kartikeya M / Opalko, Hannah / Duennwald, Martin L / Moseley, James B / Supattapone, Surachai

mBio

2016 Volume 7, Issue 5

Abstract: Proteins containing polyglutamine (polyQ) regions are found in almost all eukaryotes, albeit with various frequencies. In humans, proteins such as huntingtin (Htt) with abnormally expanded polyQ regions cause neurodegenerative diseases such as Huntington' ...

Abstract	Proteins containing polyglutamine (polyQ) regions are found in almost all eukaryotes, albeit with various frequencies. In humans, proteins such as huntingtin (Htt) with abnormally expanded polyQ regions cause neurodegenerative diseases such as Huntington's disease (HD). To study how the presence of endogenous polyQ aggregation modulates polyQ aggregation and toxicity, we expressed polyQ expanded Htt fragments (polyQ Htt) in Schizosaccharomyces pombe In stark contrast to other unicellular fungi, such as Saccharomyces cerevisiae, S. pombe is uniquely devoid of proteins with more than 10 Q repeats. We found that polyQ Htt forms aggregates within S. pombe cells only with exceedingly long polyQ expansions. Surprisingly, despite the presence of polyQ Htt aggregates in both the cytoplasm and nucleus, no significant growth defect was observed in S. pombe cells. Further, PCR analysis showed that the repetitive polyQ-encoding DNA region remained constant following transformation and after multiple divisions in S. pombe, in contrast to the genetic instability of polyQ DNA sequences in other organisms. These results demonstrate that cells with a low content of polyQ or other aggregation-prone proteins can show a striking resilience with respect to polyQ toxicity and that genetic instability of repetitive DNA sequences may have played an important role in the evolutionary emergence and exclusion of polyQ expansion proteins in different organisms. Importance: Polyglutamine (polyQ) proteins encoded by repetitive CAG DNA sequences serve a variety of normal biological functions. Yet some proteins with abnormally expanded polyQ regions cause neurodegeneration through unknown mechanisms. To study how distinct cellular environments modulate polyQ aggregation and toxicity, we expressed CAG-expanded huntingtin fragments in Schizosaccharomyces pombe In stark contrast to many other eukaryotes, S. pombe is uniquely devoid of proteins containing long polyQ tracts. Our results show that S. pombe cells, despite their low content of endogenous polyQ proteins, exhibit striking and unexpected resilience with respect to polyQ toxicity and that genetic instability of repetitive DNA sequences may have played an important role in the emergence and expansion of polyQ domains in eukaryotic evolution.
Language	English
Publishing date	2016-09-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mBio.01367-16
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Article ; Online: Ploidy variation in multinucleate cells changes under stress.

Anderson, Cori A / Roberts, Samantha / Zhang, Huaiying / Kelly, Courtney M / Kendall, Alexxy / Lee, ChangHwan / Gerstenberger, John / Koenig, Aaron B / Kabeche, Ruth / Gladfelter, Amy S

Molecular biology of the cell

2015 Volume 26, Issue 6, Page(s) 1129–1140

Abstract: Ploidy variation is found in contexts as diverse as solid tumors, drug resistance in fungal infection, and normal development. Altering chromosome or genome copy number supports adaptation to fluctuating environments but is also associated with fitness ... ...

Abstract	Ploidy variation is found in contexts as diverse as solid tumors, drug resistance in fungal infection, and normal development. Altering chromosome or genome copy number supports adaptation to fluctuating environments but is also associated with fitness defects attributed to protein imbalances. Both aneuploidy and polyploidy can arise from multinucleate states after failed cytokinesis or cell fusion. The consequences of ploidy variation in syncytia are difficult to predict because protein imbalances are theoretically buffered by a common cytoplasm. We examined ploidy in a naturally multinucleate fungus, Ashbya gossypii. Using integrated lac operator arrays, we found that chromosome number varies substantially among nuclei sharing a common cytoplasm. Populations of nuclei range from 1N to >4N, with different polyploidies in the same cell and low levels of aneuploidy. The degree of ploidy variation increases as cells age. In response to cellular stress, polyploid nuclei diminish and haploid nuclei predominate. These data suggest that mixed ploidy is tolerated in these syncytia; however, there may be costs associated with variation as stress homogenizes the genome content of nuclei. Furthermore, the results suggest that sharing of gene products is limited, and thus there is incomplete buffering of ploidy variation despite a common cytosol.
MeSH term(s)	Ascomycota/cytology ; Ascomycota/genetics ; Ascomycota/growth & development ; Cell Nucleus/genetics ; Chromosome Segregation ; Chromosomes, Fungal/genetics ; DNA, Fungal/genetics ; Fungal Proteins/physiology ; Gene Dosage ; Genes, Fungal ; Mad2 Proteins/physiology ; Polyploidy ; Stress, Physiological
Chemical Substances	DNA, Fungal ; Fungal Proteins ; Mad2 Proteins
Language	English
Publishing date	2015-03-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E14-09-1375
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Article ; Online: CAG Expansions Are Genetically Stable and Form Nontoxic Aggregates in Cells Lacking Endogenous Polyglutamine Proteins

Ashley A. Zurawel / Ruth Kabeche / Sonja E. DiGregorio / Lin Deng / Kartikeya M. Menon / Hannah Opalko / Martin L. Duennwald / James B. Moseley / Surachai Supattapone

mBio, Vol 7, Iss 5, p e01367-

2016 Volume 16

Abstract	Proteins containing polyglutamine (polyQ) regions are found in almost all eukaryotes, albeit with various frequencies. In humans, proteins such as huntingtin (Htt) with abnormally expanded polyQ regions cause neurodegenerative diseases such as Huntington’s disease (HD). To study how the presence of endogenous polyQ aggregation modulates polyQ aggregation and toxicity, we expressed polyQ expanded Htt fragments (polyQ Htt) in Schizosaccharomyces pombe. In stark contrast to other unicellular fungi, such as Saccharomyces cerevisiae, S. pombe is uniquely devoid of proteins with more than 10 Q repeats. We found that polyQ Htt forms aggregates within S. pombe cells only with exceedingly long polyQ expansions. Surprisingly, despite the presence of polyQ Htt aggregates in both the cytoplasm and nucleus, no significant growth defect was observed in S. pombe cells. Further, PCR analysis showed that the repetitive polyQ-encoding DNA region remained constant following transformation and after multiple divisions in S. pombe, in contrast to the genetic instability of polyQ DNA sequences in other organisms. These results demonstrate that cells with a low content of polyQ or other aggregation-prone proteins can show a striking resilience with respect to polyQ toxicity and that genetic instability of repetitive DNA sequences may have played an important role in the evolutionary emergence and exclusion of polyQ expansion proteins in different organisms.
Keywords	Science ; Q ; Microbiology ; QR1-502
Subject code	612
Language	English
Publishing date	2016-09-01T00:00:00Z
Publisher	American Society for Microbiology
Document type	Article ; Online
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