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	Sup35p - Wikipedia, the free encyclopedia
		Sup35p is the Saccharomyces cerevisiae (a yeast) eukaryotic translation termination factor.
		Partial loss of function results in nonsense suppression, in which stop codons are ignored and proteins are abnormally synthesized with carboxyl terminal extensions.
		Sup35p is an intensely studied protein because it can propagate in a prion form, resulting in the [PSI+] phenotype.
	en.wikipedia.org /wiki/Sup35p (177 words)

	SUP35 -
		We propose that Sup45p and Sup35p interact to form a release factor complex in yeast and that Sup35p, which has GTP binding sequence motifs in its C-terminal domain, provides the GTP hydrolytic activity which is a demonstrated requirement of the eukaryote translation termination reaction.
		The dsup35(63D) mutation is caused by a P element insertion that affects, specifically in the testis, the expression of a gene (dsup35) encoding the Drosophila homolog of the yeast Sup35p and Xenopus eRF3 proteins.
		The prion-like properties of yeast Sup35p and Ure2p proteins and a role of tandem amino acid repeats localized in N-terminal region of Sup35p protein in inheritance of [psi] determinants is discussed.
	www.ihop-net.org /UniPub/iHOP/gg/32180.html (5329 words)

	The Yeast [PSI+] Prion: Making Sense of Nonsense -- Liebman and Derkatch 274 (3): 1181 -- Journal of Biological ...
		The N domain of Sup35p (amino acids 1-123) is shown in blue, the highly charged M domain (amino acids 124-253) in yellow, and the C domain (amino acids 254-685) in red.
		the yeast Sup45p is an eRF1 whereas Sup35p is an eRF3 (42-44).
		Sup35p may have functions distinct from its role in the termination of translation.
	www.jbc.org /cgi/content/full/274/3/1181 (4213 words)

	Interaction between yeast Sup45p ( eRF1) and Sup35p ( eRF3) polypeptide chain release factors: implications for ...
		Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation.It has been suggested that the Sup35 protein (Sup35p) is subject to a heritable conformational switch, similar to mammalian prions, thus giving rise to the non-Mendelian [PSI+] nonsense suppressor determinant.
		Sup35p is composed of the N-terminal domain (N) required for [PSI+] maintenance, the presumably nonfunctional middle region (M), and the C-terminal domain (C) essential for translation termination.
		The N domain of Sup35p, responsible for its aggregation in [PSI+] cells, may thus act as a repressor of another polypeptide chain release factor, Sup45p.
	www.ihop-net.org /UniPub/iHOP/gp/984099.html (262 words)

	Full Article
		The Sup35p was shown to contain two functionally distinct domains: N domain (the sequence of first 123 amino acids) and C domain (amino acids 254-685).
		This mutation does not affect the binding of Sup35p molecules to the prion aggregate, but decreases the efficiency of its subsequent conformational rearrangement and/or the efficiency of binding of the next molecule of Sup35p [58].
		Therefore, the prion state of the Sup35p allows "fine tuning" of the translation termination efficiency according to the environmental conditions; this may be of adaptive importance for the yeast.
	www.protein.bio.msu.ru /biokhimiya/contents/v64/full/64121638.html (6195 words)

	The Rochet Lab (Purdue University) \| Jamie's Research Page
		The prion state of Sup35p is investigated using a strain of Saccharomyces cerevisiae engineered to express the ade1-14 allele that encodes a nonsense codon in the coding region of the ADE1 gene encoding an essential enzyme in the biosynthetic pathway of adenine (9).
		In [psi-] yeast (A), Sup35p is soluble and active as a translation termination factor.
		In [PSI+] yeast (B), Sup35p is insoluble (prion state) due to extensive interactions at the N-terminal domain, translation termination is suppressed and partial readthrough of the ADE1 gene occurs.
	people.pharmacy.purdue.edu /~rochet/doranlab.shtml (1277 words)

	Dissection and Design of Yeast Prions
		Schematic Diagram of Sup35p and New1pPrion domains of both proteins are enlarged in the center, highlighting the Q/N-rich tract of Sup35p (blue), the NYN tripeptide repeat of New1p (purple), and the oligopeptide repeat sequences (orange) found in both proteins.
		Sup35p can alternate between a biochemically active, soluble form ([psi–]) and an aggregated prion state ([PSI+]) with diminished translation termination activity, which can be monitored by nonsense suppression of the mutant ade1–14 allele (Liebman and Derkatch 1999).
		A Sup35p inducer containing the PNM2-1 (G58D) mutation was overexpressed in [psi–] [PIN+] cells; shown are cells (inset) with representative fluorescent foci, which were the same in frequency and appearance as cells with a wild-type inducer.
	www.cs.neu.edu /home/futrelle/bionlp/RPF/exampleDocs/prionPaper/PrionTokenNumbered6.html (4012 words)

	The ELSO Gazette Reviews (Site not responding. Last check: 2007-11-03)
		] propagation in vivo and on the aggregation of Sup35p in vitro.
		This region may therefore define a major determinant of the ‘species barrier’ in Sup35p propagation, although it is extremely unlikely that there is transfer of either soluble or aggregated Sup35p between different yeast species, not least because Sup35p is a cytoplasmic protein.
		Full-length Sup35p is difficult to generate in a soluble recombinant form on the scale needed for such studies.
	www.the-elso-gazette.org /magazines/issue7/reviews/reviews1.asp (5433 words)

	Role for Hsp70 Chaperone in Saccharomyces cerevisiae Prion Seed Replication -- Song et al. 4 (2): 289 -- Eukaryotic Cell
		of Sup35p that propagates as self-replicating cytoplasmic aggregates.
		Sup35p is a translation termination factor that catalyzes release
		Cells expressing NGMC in place of endogenous Sup35p were grown on YPAD plates at 30° for 1, 2, and 4 days (1d, 2d, and 4d, respectively).
	ec.asm.org /cgi/content/full/4/2/289 (5517 words)

	Prions in Saccharomyces and Podospora spp.: Protein-Based Inheritance -- Wickner et al. 63 (4): 844 -- Microbiology and ...
		The prion domains of Ure2p and Sup35p are rich in Asn and Gln residues, and these residues are important in prion generation and propagation.
		Sup35p (14) or by facilitating the segregation of the aggregated
		Sup35p is one of two subunits of the translation termination factor, the other being Sup45p.
	mmbr.asm.org /cgi/content/full/63/4/844 (9142 words)

	Odd Prion Allele Found In Goat
		Sup35p fibers are similar to amyloid fibers associated with certain human diseases because they bind Congo red [this is of far less interest than CR birefringence -- webmaster] and are rich in -sheet structure.
		Indeed, the Sup35p fibers formed in vitro have been shown to exist in distinct structural forms, "wavy" or "straight," and transitions between these forms are not observed within the same fiber, indicating that they may represent a structural basis for Psi+ variants.
		The analysis of Sup35p homologs from humans (53), Xenopus laevis (44), Podospora anserina (54), and Pichia pinus (55) suggests that the C-terminal region of Sup35p is highly conserved (approximately 60% similarity between different species), and it is generally assumed to function as eRF3 in all eukaryotes.
	www.mad-cow.org /jan99_mid_sci.html (6812 words)

	Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+] ...
		In inter-specific comparisons of Sup35p amino acid sequences, N and M are less conserved than C (7, 17).
		Insolubility is a characteristic of Sup35p in the [PSI
		was insoluble (as was WT Sup35p) in the heterozygous [PSI
	www.pnas.org /cgi/content/full/99/suppl_4/16446 (5157 words)

	Willkommen im Fiberlab
		One of the yeast prion proteins is the translation termination factor Sup35p of Saccharomyces cerevisiae.
		Although Sup35p lacks the respective Histidine residues in the oligopeptide repeats, we determined that Sup35p-NM is able to specifically bind copper.
		A) A) The yeast prion Sup35p: the aminoterminal region N with the oligopeptide repeats is the prion determining region, the middle region M is characterized by its high amount of charged amino acids and the carboxyterminal part C is responsible for the translation termination activity.
	www.fiberlab.de /research/yeast/yeast_topic.html (406 words)

	Yeast chaperones interact with human prions
		EMBO J 1996 Jun 17;15(12):3127-3134 Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD The Sup35p protein of yeast Saccharomyces cerevisiae is a homologue of the polypeptide chain release factor 3 (eRF3) of higher eukaryotes.
		N-terminally altered Sup35p molecules are unable to interact with the PSI+ Sup35p isoform, remain soluble and improve the translation termination in PSI+ strains, thus causing an antisuppressor phenotype.
		Structure and functional similarity of yeast Sup35p and Ure2p proteins to mammalian prions Mol Biol (Mosk) 1995 Jul;29(4):750-755[Article in Russian] Kushnirov VV, Ter-Avanesian MD, Smirnov VN The results of studies of yeast cytoplasmically-inherited determinants [psi] and [URE3] are summarized.
	www.mad-cow.org /chaperones.html (6760 words)

	Prions
		As predicted by the prion model, overproduction of Sup35p induces the de novo appearance of [PSI+].
		Unlike [PSI+], [PIN+] is not located in the N-terminal region of Sup35p and may either be a self-propagating determinant in the C-proximal part of Sup35p, or a prion domain in another protein that facilitates Sup35p conformational changes (55).
		The molecular basis of the [PIN+] factor is unknown and could involve a prion form of a general molecular chaperone, a prion protein that exclusively affects Sup35p conformational liability, or a new Sup35p prion variant distinct from [PSI+] and determined by the conformation of a region in the C-proximal part of Sup35p (55).
	www.mad-cow.org /mar98_sci.html (5117 words)

	A Role for Cytosolic Hsp70 in Yeast [PSI+] Prion Propagation and [PSI+] as a Cellular Stress -- Jung et al. 156 (2): ...
		Sup35p is a Saccharomyces cerevisiae protein involved in termination
		For both strains, exposures were selected in which the intensity of the signal of Sup35p in the pellet fractions is similar.
		Hsp104 is regulating the solubility of Sup35p in environmentally
	www.genetics.org /cgi/content/full/156/2/559 (5614 words)

	YGM-2003: Abstract 18-47 (Site not responding. Last check: 2007-11-03)
		Sup35p to its prion form; or Hsp104 disaggregates the Sup35p prion aggregates to produce many and smaller aggregates which facilitate partitioning and then transmission to daughter cells.
		Consequently, in the absence of Hsp104, fewer and larger Sup35p aggregates accumulate that would decrease their chance of transmission to daughter cells.
		This effect, which is specific to the Sup35p prion, may highlight the particular role of Hsp104 in linking the translation termination factor Sup35p (eRF3) to subcellular structures (e.g.
	www.yeastgenome.org /community/meetings/yeast03/abshtml/18-47.html (251 words)

	intas 94-2960 (Site not responding. Last check: 2007-11-03)
		A homologous cell-free translation system that is dependent on the SUP35p protein will be generated in order to estimate its role in protein synthesis.
		On the other hand, the identification of genes which interact with SUP35 will be undertaken; this can be done either by searching for genes, the expression of which is under the control of the SUP35 gene product, or by identifying physically interacting components.
		In addition, Sup35p N-terminal domain may act as a trans-acting repressor of another polypeptide chain release factor, Sup45p.
	www.intas.be /catalog/94-2960.htm (775 words)

	Prions: proteins as genes and infectious entities -- Wickner et al. 18 (5): 470 -- Genes and Development
		Sequestration of Ure2p or Sup35p in amyloid filaments impairs their availability to carry out their normal functions in nitrogen regulation and translation termination, respectively.
		Whereas the prion domains of Ure2p and Sup35p are N/Q rich, those of PrP and HET-s are not.
		Sup35p in aggregates (presumed to be amyloid filaments) is not
	www.genesdev.org /cgi/content/full/18/5/470 (6849 words)

	ALS TDF
		Here we demonstrate that the rate of incorporation of newly synthesized Sup35p into the high-molecular-weight aggregates, diagnostic of [PSI(+)] strains, is proportional to the number of seeds in the cell, with seed number declining (and the levels of soluble Sup35p increasing) in the presence of GdnHCl.
		Transfer of GdnHCl-treated cells to GdnHCl-free medium reverses GdnHCl inhibition of [PSI(+)] seed replication and allows new prion seeds to be generated exponentially in the absence of ongoing protein synthesis.
		Based on these and other data, we propose a two-cycle model for "prionization" of Sup35p in [PSI(+)] cells: cycle A is the GdnHCl-sensitive (Hsp104-dependent) replication of the prion seeds, while cycle B is a GdnHCl-insensitive (Hsp104-independent) process that converts these seeds to pelletable aggregates.
	www.als.net /articles/articleDetail.asp?articleId=2433 (314 words)

	Antagonistic Interactions between Yeast [PSI+] and [URE3] Prions and Curing of [URE3] by Hsp70 Protein Chaperone Ssa1p ...
		Immediately (lanes 1 and 2), 2 h (lanes 3 and 4), and 6 h (lanes 5 and 6) after transfer to SG medium, cells were removed and assayed for Sup35p abundance as described in Materials and Methods.
		Transient overexpression of Sup35p or Ure2p in yeast significantly
		] inducibility by overproduced Sup35p in the absence of
	mcb.asm.org /cgi/content/full/22/11/3590 (4927 words)

	PhD \| Project Details \| Printer Friendly Page (Site not responding. Last check: 2007-11-03)
		An altered conformer of the prion protein acts as a “seed” to convert all newly synthesised molecules of that protein into the prion form.
		In our studies, we are focussing predominantly on the yeast prion protein Sup35p (otherwise known as eRF3), a subunit of the translation termination release factor.
		By studying the yeast Sup35p prion, we are obtaining important insights into how prion proteins are propagated in the eukaryotic cell, findings that can be readily extrapolated to the behaviour of the mammalian prions that give rise to neurodegenerative diseases such as CJD and BSE.
	www.findaphd.com /search/printpage.asp?projectid=1828 (306 words)

	JSWlab :: Research
		My laboratory has taken advantage of the PSI-phenomenon to identify and characterize properties of the Sup35p protein _that allow it to propagate a b-sheet rich prion form.
		We are now establishing a more general set of tools for studying amyloid formation of disease-related proteins in yeast.
		Finally, we have exploited our conservation and mutational data on Sup35p to develop algorithms for searching genomic databases for novel prion-forming proteins.
	www.ucsf.edu /jswlab/research_amyloid.html (226 words)

	Prions of Yeast and Fungi. PROTEINS AS GENETIC MATERIAL -- Wickner et al. 274 (2): 555 -- Journal of Biological ...
		Sup35p is a subunit of the translation release factor that recognizes termination codons and releases the completed peptide
		all three genetic criteria to be a prion form of Sup35p (1).
		Sup35p is necessary for the propagation of [PSI] (26, 27).
	www.jbc.org /cgi/content/full/274/2/555 (3086 words)

	Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for ...
		Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation -- Paushkin et al.
		Sup35p is composed of the N-terminal domain (N) required for [PSI+] maintenance, the presumably nonfunctional middle region
		Sup35p, responsible for its aggregation in [PSI+] cells, may thus act as a
	mcb.asm.org /cgi/content/abstract/17/5/2798 (666 words)

	The Candida albicans Sup35p protein (CaSup35p): function, prion-like behaviour and an associated polyglutamine length ... (Site not responding. Last check: 2007-11-03)
		Sup35p to the aggregated prion form is promoted by a yet-to-be
		Sup35p region did not prevent the chimaeric Sup35p from forming
		The presence of the Sup35p homologue was expected to
	mic.sgmjournals.org /cgi/content/full/148/4/1049 (5942 words)

	The non-Mendelian factor [ ETA ], like [ PSI ], is a prion-like form of Sup35p. (Site not responding. Last check: 2007-11-03)
		The non-Mendelian factor [ ETA ], like [ PSI ], is a prion-like form of Sup35p.
		However, the [ ETA ] factor was originally distinguished from [ PSI ] by its meiotic instability, its lack of nonsense suppressor activity and its compatibility with tRNA suppressors.
		], is caused by a prion form of Sup35p and is actually a [ PSI ] variant.
	www.yeastgenome.org /community/meetings/yeast98/abshtml/561.html (273 words)

	Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI+] of Saccharomyces ...
		chromosome-encoded protein Sup35p is known to be one of two eukaryote
		The calculated generation times for both sets of data from the model were within 10% of the experimentally determined generation times.
		Sup35p can be eliminated by growth in the presence of millimolar
	www.pnas.org /cgi/content/full/97/1/240 (4592 words)

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