Constitutive Flocculation inSaccharomyces cerevisiae Through Overexpression of theGTS1 Gene, coding for a ‘Glo’-type Zn-finger-containing Protein

Bossier, Peter; Goethals, Peter; Rodrigues-Pousada, Claudina

doi:10.1002/(sici)1097-0061(19970630)13:8<717::aid-yea132>3.0.co;2-2

Cited by 25 publications

(21 citation statements)

References 27 publications

(9 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1C). Gts1p is a nonessential transcription factor that has been implicated in several processes including the stress response, sporulation, and the cell cycle (39,40). Gts1p was erroneously thought to contain glycine/threonine-serine repeats, but instead contains a Q-rich region including an imperfect glutamine-alanine repeat (QAR) in its C-terminal domain ( Fig.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome

Ripaud¹,

Chumakova²,

Antonin³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Expansion of a poly-glutamine (polyQ) repeat in a group of functionally unrelated proteins is the cause of several inherited neurodegenerative disorders, including Huntington's disease. The polyQ length-dependent aggregation and toxicity of these disease proteins can be reproduced in Saccharomyces cerevisiae. This system allowed us to screen for genes that when overexpressed reduce the toxic effects of an N-terminal fragment of mutant huntingtin with 103 Q. Surprisingly, among the identified suppressors were three proteins with Q-rich, prion-like domains (PrDs): glycine threonine serine repeat protein (Gts1p), nuclear polyadenylated RNA-binding protein 3, and minichromosome maintenance protein 1. Overexpression of the PrD of Gts1p, containing an imperfect 28 residue glutamine-alanine repeat, was sufficient for suppression of toxicity. Association with this discontinuous polyQ domain did not prevent 103Q aggregation, but altered the physical properties of the aggregates, most likely early in the assembly pathway, as reflected in their increased SDS solubility. Molecular simulations suggested that Gts1p arrests the aggregation of polyQ molecules at the level of nonfibrillar species, acting as a cap that destabilizes intermediates on path to form large fibrils. Quantitative proteomic analysis of polyQ interactors showed that expression of Gts1p reduced the interaction between polyQ and other prion-like proteins, and enhanced the association of molecular chaperones with the aggregates. These findings demonstrate that short, Q-rich peptides are able to shield the interactive surfaces of toxic forms of polyQ proteins and direct them into nontoxic aggregates.protein aggregation | protein misfolding | neurodegeneration | prion | polyglutamine proteins

show abstract

Section: Resultsmentioning

confidence: 99%

“…2A). Gts1p also contains a Zn-finger motif and an ubiquitinassociated (UBA) domain (40). The Q-rich sequences of the three suppressors differ from those of bona fide prion domains in proteins such as the eukaryotic release factor Sup35p in that they are not enriched in asparagine (N) ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome

Ripaud¹,

Chumakova²,

Antonin³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…The mechanism behind the flocculation induction in such different situations is far from being understood. More recently, the overexpression of the GTS1 gene has been reported to result in constitutive flocculation [98], even when expressed in a yeast strain lacking the FLO1 gene, suggesting that the flocculation mediated by these two genes is unlinked. Overexpression of GTS1 results in an increase of thermotolerance (broadening the tempera-ture growth optimum and increasing lethal heat shock resistance) and in a change in the cell wall long-chain fatty acids profile (leading to a reduced cell surface charge and increased hydrophobicity).…”

Section: Genetics Of Yeast Flocculationmentioning

confidence: 98%

“…It is likely that the flocculation mechanism of these strains is different from the Flo1 and NewFlo mechanism. The GTS1 overexpression could be related to this type of flocculation since an increase in hydrophobicity has been noticed [98]. However, further data are required.…”

Section: Genetics Of Yeast Flocculationmentioning

confidence: 99%

Applications of yeast flocculation in biotechnological processes

Domingues

Vicente

Lima

et al. 2000

Biotechnol. Bioprocess Eng.

View full text Add to dashboard Cite

A review on the main aspects associated with yeast flocculation and its application in biotechnological processes is presented. This subject is addressed following three main aspects -the basics of yeast flocculation, the development of "new" flocculating yeast strains and bioreactor development. In what concerns the basics of yeast flocculation, the state of the art on the most relevant aspects of mechanism, physiology and genetics of yeast flocculation is reported. The construction of flocculating yeast strains includes not only the recombinant constitutive flocculent brewer's yeast, but also recombinant flocculent yeast for lactose metabolisation and ethanol production. Furthermore, recent work on the heterologous β-galactosidase production using a recombinant flocculent Saccharomyces cerevisiae is considered. As bioreactors using flocculating yeast cells have particular properties, mainly associated with a high solid phase hold-up, a section dedicated to its operation is presented. Aspects such as bioreactor productivity and culture stability as well as bioreactor hydrodynamics and mass transfer properties of flocculating cell cultures are considered. Finally, the paper concludes describing some of the applications of high cell density flocculation bioreactors and discussing potential new uses of these systems.

show abstract

“…These genes, together with FLO1, FLO5 and FLO8, are now considered the`¯occulin family' and encode for proteins with a high degree of homology (Bossier et al, 1997;Teunissen and Steensma, 1995). In 1996, Lo and Draginis reported a new¯occulin, encoded by FLO11, a yeast gene related to STA genes, and later Sieiro et al (1997) cloned a¯occulation-conferring gene (FLO2) that was able to complement the¯o1 mutation.…”

Section: Introductionmentioning

confidence: 99%

Flocculation of Saccharomyces cerevisiae is induced by transformation with the GAP1 gene from Kluyveromyces marxianus

Moreira¹,

Ferreira‐da‐Silva²,

Fernandes

et al. 2000

Yeast

View full text Add to dashboard Cite

A non-¯occulent strain of Saccharomyces cerevisiae was transformed with the GAP1 gene which encodes p37, a GAPDH-like protein present in the cell wall of Kluyveromyces marxianus¯occulent cells. The transformed cells were characterized with respect to¯occulation behaviour, morphology, growth, cell wall integrity and GAPDH activity. A¯occulent phenotype was acquired by the transformed cells, showing a behaviour in respect tō occulation/de¯occulation very similar to that of K. marxianus. The presence of p37 in the cell wall was assessed by immunoprecipitation of biotinylated cell wall proteins and an accumulation of p37 was evident in the cell wall of transformed cells. This result was con®rmed by studies using a chimeric protein resulting from fusing the p37 with a yeast-enhanced green¯uorescent protein, yEGFP. The recombinant protein was localized mainly in the cell wall of the transformed strain, although the presence of p37 in the cytosol was indicated by an increase in GAPDH activity. Calco¯uor white sensitivity tests indicated that the cell wall structure is affected by the accumulation of p37. These results provided further evidence of p37 function regarding¯occulation and that although lacking a N-terminal signal peptide p37 is targeted to the cell wall.

show abstract

Constitutive Flocculation inSaccharomyces cerevisiae Through Overexpression of theGTS1 Gene, coding for a ‘Glo’-type Zn-finger-containing Protein

Cited by 25 publications

References 27 publications

Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome

Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome

Applications of yeast flocculation in biotechnological processes

Flocculation of Saccharomyces cerevisiae is induced by transformation with the GAP1 gene from Kluyveromyces marxianus

Contact Info

Product

Resources

About