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https://www.readbyqxmd.com/read/28721580/gene-expression-profiles-of-the-thermotolerant-yeast-saccharomyces-cerevisiae-strain-kku-vn8-during-high-temperature-ethanol-fermentation-using-sweet-sorghum-juice
#1
Atiya Techaparin, Pornthap Thanonkeo, Preekamol Klanrit
OBJECTIVES: To investigate gene expression profiles of the thermotolerant yeast Saccharomyces cerevisiae strain KKU-VN8, a potential high-ethanol producer, in response to various stresses during high-temperature ethanol fermentation using sweet sorghum juice (SSJ) under optimal conditions. RESULTS: The maximal ethanol concentration obtained by S. cerevisiae KKU-VN8 using SSJ at 40 °C was 66.6 g/l, with a productivity of 1.39 g/l/h and a theoretical ethanol yield of 81%...
July 18, 2017: Biotechnology Letters
https://www.readbyqxmd.com/read/28666328/amyotrophic-lateral-sclerosis-related-mutant-superoxide-dismutase-1-aggregates-inhibit-14-3-3-mediated-cell-survival-by-sequestration-into-the-junq-compartment
#2
Ju-Hwang Park, Hae Rim Jang, In Young Lee, Hye Kyung Oh, Eui-Ju Choi, Hyangshuk Rhim, Seongman Kang
Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disorder characterized by motor neuron loss in the spinal cord and brain. Mutations in the superoxide dismutase 1 (SOD1) gene have been linked to familial ALS. To elucidate the role of SOD1 mutations in ALS, we investigated 14-3-3, a crucial regulator of cell death that was identified in patients with familial ALS. In a transgenic mouse model (SOD1-G93A) of ALS, 14-3-3 co-localized with mutant SOD1 aggregates and was more insoluble in the spinal cords of mutant SOD1 transgenic mice than in those of wild-type mice...
June 28, 2017: Human Molecular Genetics
https://www.readbyqxmd.com/read/28653109/the-life-of-psi
#3
REVIEW
Brian Cox, Mick Tuite
The AAA+ disaggregase Hsp104 is essential for the maintenance and inheritance of nearly all known prions of the yeast Saccharomyces cerevisiae. Uniquely for [PSI (+)], the prion form of the Sup35 protein, there seem to be two activities, involving differing co-chaperones, by which Hsp104 affects the inheritance of [PSI (+)], the prion form of the Sup35 protein. Each pathway is also involved in protection against ageing, one through disaggregation of damaged proteins and the other through their retention in the mother cell during budding...
June 26, 2017: Current Genetics
https://www.readbyqxmd.com/read/28632741/aging-mortality-and-the-fast-growth-trade-off-of-schizosaccharomyces-pombe
#4
Hidenori Nakaoka, Yuichi Wakamoto
Replicative aging has been demonstrated in asymmetrically dividing unicellular organisms, seemingly caused by unequal damage partitioning. Although asymmetric segregation and inheritance of potential aging factors also occur in symmetrically dividing species, it nevertheless remains controversial whether this results in aging. Based on large-scale single-cell lineage data obtained by time-lapse microscopy with a microfluidic device, in this report, we demonstrate the absence of replicative aging in old-pole cell lineages of Schizosaccharomyces pombe cultured under constant favorable conditions...
June 2017: PLoS Biology
https://www.readbyqxmd.com/read/28626006/atairp2-e3-ligase-affects-aba-and-high-salinity-responses-by-stimulating-its-atp1-sdirip1-substrate-turnover
#5
Tae Rin Oh, Jong Hum Kim, Seok Keun Cho, Moon Young Ryu, Seong Wook Yang, Woo Taek Kim
AtAIRP2 is a cytosolic RING-type E3 ubiquitin (Ub) ligase that positively regulates an ABA response in Arabidopsis (Arabidopsis thaliana). Yeast two-hybrid screening using AtAIRP2 as bait identified ATP1 (AtAIRP2 Target Protein 1) as a substrate of AtAIRP2. ATP1 was found to be identical to SDIRIP1, which was recently reported to be a negative factor in ABA signaling and a target protein of the RING E3 ligase SDIR1. ATP1 was accordingly renamed ATP1/SDIRIP1. A specific interaction between AtAIRP2 and ATP1/SDIRIP1 and ubiquitination of ATP1/SDIRIP1 by AtAIRP2 were demonstrated in vitro and in planta...
June 16, 2017: Plant Physiology
https://www.readbyqxmd.com/read/28619716/ratchet-like-polypeptide-translocation-mechanism-of-the-aaa-disaggregase-hsp104
#6
Stephanie N Gates, Adam L Yokom, JiaBei Lin, Meredith E Jackrel, Alexandrea N Rizo, Nathan M Kendsersky, Courtney E Buell, Elizabeth A Sweeny, Korrie L Mack, Edward Chuang, Mariana P Torrente, Min Su, James Shorter, Daniel R Southworth
Hsp100 polypeptide translocases are conserved AAA+ machines that maintain proteostasis by unfolding aberrant and toxic proteins for refolding or proteolytic degradation. The Hsp104 disaggregase from S. cerevisiae solubilizes stress-induced amorphous aggregates and amyloid. The structural basis for substrate recognition and translocation is unknown. Using a model substrate (casein), we report cryo-EM structures at near-atomic resolution of Hsp104 in different translocation states. Substrate interactions are mediated by conserved, pore-loop tyrosines that contact an 80 Å-long unfolded polypeptide along the axial channel...
June 15, 2017: Science
https://www.readbyqxmd.com/read/28611991/substrate-discrimination-by-clpb-and-hsp104
#7
Danielle M Johnston, Marika Miot, Joel R Hoskins, Sue Wickner, Shannon M Doyle
ClpB of E. coli and yeast Hsp104 are homologous molecular chaperones and members of the AAA+ (ATPases Associated with various cellular Activities) superfamily of ATPases. They are required for thermotolerance and function in disaggregation and reactivation of aggregated proteins that form during severe stress conditions. ClpB and Hsp104 collaborate with the DnaK or Hsp70 chaperone system, respectively, to dissolve protein aggregates both in vivo and in vitro. In yeast, the propagation of prions depends upon Hsp104...
2017: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/28611990/structure-and-function-of-p97-and-pex1-6-type-ii-aaa-complexes
#8
REVIEW
Paul Saffert, Cordula Enenkel, Petra Wendler
Protein complexes of the Type II AAA+ (ATPases associated with diverse cellular activities) family are typically hexamers of 80-150 kDa protomers that harbor two AAA+ ATPase domains. They form double ring assemblies flanked by associated domains, which can be N-terminal, intercalated or C-terminal to the ATPase domains. Most prominent members of this family include NSF (N-ethyl-maleimide sensitive factor), p97/VCP (valosin-containing protein), the Pex1/Pex6 complex and Hsp104 in eukaryotes and ClpB in bacteria...
2017: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/28574745/prion-specific-hsp40-function-the-role-of-the-auxilin-homolog-swa2
#9
Emily E Oliver, Elizabeth M Troisi, Justin K Hines
Yeast prions are protein-based genetic elements that propagate through cell populations via cytosolic transfer from mother to daughter cell. Molecular chaperone proteins including Hsp70, the Hsp40/J-protein Sis1, and Hsp104 are required for continued prion propagation, however the specific requirements of chaperone proteins differ for various prions. We recently reported that Swa2, the yeast homolog of the mammalian protein auxilin, is specifically required for the propagation of the prion [URE3]. (1) [URE3] propagation requires both a functional J-domain and the tetratricopeptide repeat (TPR) domain of Swa2, but does not require Swa2 clathrin binding...
May 4, 2017: Prion
https://www.readbyqxmd.com/read/28527764/differential-stress-response-of-saccharomyces-hybrids-revealed-by-monitoring-hsp104-aggregation-and-disaggregation
#10
Claudia Kempf, Klaus Lengeler, Jürgen Wendland
Proteotoxic stress may occur upon exposure of yeast cells to different stress conditions. The induction of stress response mechanisms is important for cells to adapt to changes in the environment and ensure survival. For example, during exposure to elevated temperatures the expression of heat shock proteins such as Hsp104 is induced in yeast. Hsp104 extracts misfolded proteins from aggregates to promote their refolding. We used an Hsp104-GFP reporter to analyze the stress profiles of Saccharomyces species hybrids...
July 2017: Microbiological Research
https://www.readbyqxmd.com/read/28484020/hsp104-disaggregase-at-normal-levels-cures-many-psi-prion-variants-in-a-process-promoted-by-sti1p-hsp90-and-sis1p
#11
Anton Gorkovskiy, Michael Reidy, Daniel C Masison, Reed B Wickner
Overproduction or deficiency of many chaperones and other cellular components cure the yeast prions [PSI(+)] (formed by Sup35p) or [URE3] (based on Ure2p). However, at normal expression levels, Btn2p and Cur1p eliminate most newly arising [URE3] variants but do not cure [PSI(+)], even after overexpression. Deficiency or overproduction of Hsp104 cures the [PSI(+)] prion. Hsp104 deficiency curing is a result of failure to cleave the Sup35p amyloid filaments to make new seeds, whereas Hsp104 overproduction curing occurs by a different mechanism...
May 23, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28389532/rna-binding-proteins-with-prion-like-domains-in-health-and-disease
#12
REVIEW
Alice Ford Harrison, James Shorter
Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD). PrLDs are low-complexity domains that possess a similar amino acid composition to prion domains in yeast, which enable several proteins, including Sup35 and Rnq1, to form infectious conformers, termed prions. In humans, PrLDs contribute to RBP function and enable RBPs to undergo liquid-liquid phase transitions that underlie the biogenesis of various membraneless organelles. However, this activity appears to render RBPs prone to misfolding and aggregation connected to neurodegenerative disease...
April 7, 2017: Biochemical Journal
https://www.readbyqxmd.com/read/28379007/avidity-for-polypeptide-binding-by-nucleotide-bound-hsp104-structures
#13
Clarissa L Weaver, Elizabeth C Duran, Korrie L Mack, JiaBei Lin, Meredith E Jackrel, Elizabeth A Sweeny, James Shorter, Aaron L Lucius
Recent Hsp104 structural studies have reported both planar and helical models of the hexameric structure. The conformation of Hsp104 monomers within the hexamer is affected by nucleotide ligation. After nucleotide-driven hexamer formation, Hsp104-catalyzed disruption of protein aggregates requires binding to the peptide substrate. Here, we examine the oligomeric state of Hsp104 and its peptide binding competency in the absence of nucleotide and in the presence of ADP, ATPγS, AMPPNP, or AMPPCP. Surprisingly, we found that only ATPγS facilitates avid peptide binding by Hsp104...
April 18, 2017: Biochemistry
https://www.readbyqxmd.com/read/28375147/crystal-structures-of-hsp104-n-terminal-domains-from-saccharomyces-cerevisiae-and-candida-albicans-suggest-the-mechanism-for-the-function-of-hsp104-in-dissolving-prions
#14
Peng Wang, Jingzhi Li, Clarissa Weaver, Aaron Lucius, Bingdong Sha
Hsp104 is a yeast member of the Hsp100 family which functions as a molecular chaperone to disaggregate misfolded polypeptides. To understand the mechanism by which the Hsp104 N-terminal domain (NTD) interacts with its peptide substrates, crystal structures of the Hsp104 NTDs from Saccharomyces cerevisiae (ScHsp104NTD) and Candida albicans (CaHsp104NTD) have been determined at high resolution. The structures of ScHsp104NTD and CaHsp104NTD reveal that the yeast Hsp104 NTD may utilize a conserved putative peptide-binding groove to interact with misfolded polypeptides...
April 1, 2017: Acta Crystallographica. Section D, Structural Biology
https://www.readbyqxmd.com/read/28373280/heat-shock-protein-104-hsp104-mediated-curing-of-psi-yeast-prions-depends-on-both-psi-conformation-and-the-properties-of-the-hsp104-homologs
#15
Xiaohong Zhao, Ramon Rodriguez, Rebecca E Silberman, Joseph M Ahearn, Sheela Saidha, Kaelyn C Cummins, Evan Eisenberg, Lois E Greene
Prions arise from proteins that have two possible conformations: properly folded and non-infectious or misfolded and infectious. The [PSI(+)] yeast prion, which is the misfolded and self-propagating form of the translation termination factor eRF3 (Sup35), can be cured of its infectious conformation by overexpression of Hsp104, which helps dissolve the prion seeds. This dissolution depends on the trimming activity of Hsp104, which reduces the size of the prion seeds without increasing their number. To further understand the relationship between trimming and curing, trimming was followed by measuring the loss of GFP-labeled Sup35 foci from both strong and weak [PSI(+)] variants; the former variant has more seeds and less soluble Sup35 than the latter...
May 26, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28298410/fus-inclusions-disrupt-rna-localization-by-sequestering-kinesin-1-and-inhibiting-microtubule-detyrosination
#16
Kyota Yasuda, Sarah F Clatterbuck-Soper, Meredith E Jackrel, James Shorter, Stavroula Mili
Cytoplasmic inclusions of the RNA-binding protein fused in sarcoma (FUS) represent one type of membraneless ribonucleoprotein compartment. Formation of FUS inclusions is promoted by amyotrophic lateral sclerosis (ALS)-linked mutations, but the cellular functions affected upon inclusion formation are poorly defined. In this study, we find that FUS inclusions lead to the mislocalization of specific RNAs from fibroblast cell protrusions and neuronal axons. This is mediated by recruitment of kinesin-1 mRNA and protein within FUS inclusions, leading to a loss of detyrosinated glutamate (Glu)-microtubules (MTs; Glu-MTs) and an inability to support the localization of RNAs at protrusions...
April 3, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28293166/protein-remodeling-factors-as-potential-therapeutics-for-neurodegenerative-disease
#17
REVIEW
Meredith E Jackrel, James Shorter
Protein misfolding is implicated in numerous neurodegenerative disorders including amyotrophic lateral sclerosis, Parkinson's disease, Alzheimer's disease, and Huntington's disease. A unifying feature of patients with these disorders is the accumulation of deposits comprised of misfolded protein. Aberrant protein folding can cause toxicity through a loss or gain of protein function, or both. An intriguing therapeutic approach to counter these disorders is the application of protein-remodeling factors to resolve these misfolded conformers and return the proteins to their native fold and function...
2017: Frontiers in Neuroscience
https://www.readbyqxmd.com/read/28289075/coordinated-hsp110-and-hsp104-activities-power-protein-disaggregation-in-saccharomyces-cerevisiae
#18
Jayasankar Mohanakrishnan Kaimal, Ganapathi Kandasamy, Fabian Gasser, Claes Andréasson
Protein aggregation is intimately associated with cellular stress and is accelerated during aging, disease, and cellular dysfunction. Yeast cells rely on the ATP-consuming chaperone Hsp104 to disaggregate proteins together with Hsp70. Hsp110s are ancient and abundant chaperones that form complexes with Hsp70. Here we provide in vivo data showing that the Saccharomyces cerevisiae Hsp110s Sse1 and Sse2 are essential for Hsp104-dependent protein disaggregation. Following heat shock, complexes of Hsp110 and Hsp70 are recruited to protein aggregates and function together with Hsp104 in the disaggregation process...
June 1, 2017: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/28275610/mutant-analysis-reveals-allosteric-regulation-of-clpb-disaggregase
#19
Kamila B Franke, Bernd Bukau, Axel Mogk
The members of the hexameric AAA+ disaggregase of E. coli and S. cerevisiae, ClpB, and Hsp104, cooperate with the Hsp70 chaperone system in the solubilization of aggregated proteins. Aggregate solubilization relies on a substrate threading activity of ClpB/Hsp104 fueled by ATP hydrolysis in both ATPase rings (AAA-1, AAA-2). ClpB/Hsp104 ATPase activity is controlled by the M-domains, which associate to the AAA-1 ring to downregulate ATP hydrolysis. Keeping M-domains displaced from the AAA-1 ring by association with Hsp70 increases ATPase activity due to enhanced communication between protomers...
2017: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/28241148/cytosolic-proteostasis-through-importing-of-misfolded-proteins-into-mitochondria
#20
Linhao Ruan, Chuankai Zhou, Erli Jin, Andrei Kucharavy, Ying Zhang, Zhihui Wen, Laurence Florens, Rong Li
Loss of proteostasis underlies ageing and neurodegeneration characterized by the accumulation of protein aggregates and mitochondrial dysfunction. Although many neurodegenerative-disease-associated proteins can be found in mitochondria, it remains unclear how mitochondrial dysfunction and protein aggregation could be related. In dividing yeast cells, protein aggregates that form under stress or during ageing are preferentially retained by the mother cell, in part through tethering to mitochondria, while the disaggregase Hsp104 helps to dissociate aggregates and thereby enables refolding or degradation of misfolded proteins...
March 16, 2017: Nature
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