scholarly journals Yeast Fps1 glycerol facilitator functions as a homotetramer

Yeast ◽  
2011 ◽  
Vol 28 (12) ◽  
pp. 815-819 ◽  
Author(s):  
Sara E. Beese-Sims ◽  
Jongmin Lee ◽  
David E. Levin
Keyword(s):  
Glycerol Facilitator

A water channel of the nematode C. elegans and its implications for channel selectivity of MIP proteins

1998 ◽  
Vol 275 (6) ◽  
pp. C1459-C1464 ◽  
Author(s):  
Michio Kuwahara ◽  
Kenichi Ishibashi ◽  
Yong Gu ◽  
Yoshio Terada ◽  
Yuji Kohara ◽  
...  
Keyword(s):  
Amino Acid ◽  
Water Channel ◽  
Genome Project ◽  
Amino Acid Residues ◽  
C Elegans ◽  
Extra Amino Acid ◽  
Urea Permeability ◽  
Glycerol Facilitator ◽  
A Genome ◽  
Channel Selectivity

A genome project focusing on the nematode Caenorhabditis elegans has demonstrated the presence of eight cDNAs belonging to the major intrinsic protein superfamily. We functionally characterized one of these cDNAs named C01G6.1. Injection of C01G6.1 cRNA increased the osmotic water permeability ( P f) of Xenopusoocytes 11-fold and the urea permeability 4.5-fold but failed to increase the glycerol permeability. It has been speculated that the MIP family may be separated into two large subfamilies based on the presence or absence of two segments of extra amino acid residues (∼15 amino acids) at the second and third extracellular loops. Because C01G6.1 (designated AQP-CE1), AQP3, and glycerol facilitator (GlpF) all have these two segments, we replaced the segments of AQP-CE1 with those of AQP3 and GlpF to identify their roles. The functional characteristics of these mutants were principally similar to that of wild-type AQP-CE1, although the values of P f and urea permeability were decreased by 39–74% and 28–65%, respectively. These results suggest that the two segments of extra amino acid residues may not contribute to channel selectivity or formation of the route for small solutes.

Glycerol facilitator GlpF and the associated aquaporin family of channels

2003 ◽  
Vol 13 (4) ◽  
pp. 424-431 ◽  
Author(s):  
Robert M Stroud ◽  
Larry JW Miercke ◽  
Joseph O’Connell ◽  
Shahram Khademi ◽  
John K Lee ◽  
...  
Keyword(s):  
Glycerol Facilitator ◽  
Aquaporin Family

Cloning and Sequencing of the Thermus aquaticus Glycerol Facilitator Gene

DNA Sequence ◽  
2002 ◽  
Vol 13 (6) ◽  
pp. 387-390
Author(s):  
Hua-Shan Huang ◽  
Kiyoshi Ito ◽  
Tadashi Yoshimoto
Keyword(s):  
Cloning And Sequencing ◽  
Thermus Aquaticus ◽  
Glycerol Facilitator

scholarly journals Osmotic Balance Regulates Cell Fusion during Mating in Saccharomyces cerevisiae

1997 ◽  
Vol 138 (5) ◽  
pp. 961-974 ◽  
Author(s):  
Jennifer Philips ◽  
Ira Herskowitz
Keyword(s):  
Cell Wall ◽  
Cell Fusion ◽  
Cell Contact ◽  
Fusion Event ◽  
Glycerol Facilitator ◽  
Fusion Defect ◽  
Osmotic Balance ◽  
Glycerol 3 Phosphate Dehydrogenase ◽  
Gpd1 Gene ◽  
Cell Cell

Successful zygote formation during yeast mating requires cell fusion of the two haploid mating partners. To ensure that cells do not lyse as they remodel their cell wall, the fusion event is both temporally and spatially regulated: the cell wall is degraded only after cell–cell contact and only in the region of cell–cell contact. To understand how cell fusion is regulated, we identified mutants defective in cell fusion based upon their defect in mating to a fus1 fus2 strain (Chenevert, J., N. Valtz, and I. Herskowitz. 1994. Genetics 136:1287–1297). Two of these cell fusion mutants are defective in the FPS1 gene, which codes for a glycerol facilitator (Luyten, K., J. Albertyn, W.F. Skibbe, B.A. Prior, J. Ramos, J.M. Thevelein, and S. Hohmann. 1995. EMBO [Eur. Mol. Biol. Organ.] J. 14:1360–1371). To determine whether inability to maintain osmotic balance accounts for the defect in cell fusion in these mutants, we analyzed the behavior of an fps1Δ mutant with reduced intracellular glycerol levels because of a defect in the glycerol-3-phosphate dehydrogenase (GPD1) gene (Albertyn, J., S. Hohmann, J.M. Thevelein, and B.A. Prior. 1994. Mol. Cell. Biol. 14:4135– 4144): deletion of GPD1 partially suppressed the cell fusion defect of fps1 mutants. In contrast, overexpression of GPD1 exacerbated the defect. The fusion defect could also be partially suppressed by 1 M sorbitol. These observations indicate that the fusion defect of fps1 mutants results from inability to regulate osmotic balance and provide evidence that the osmotic state of the cell can regulate fusion. We have also observed that mutants expressing hyperactive protein kinase C exhibit a cell fusion defect similar to that of fps1 mutants. We propose that Pkc1p regulates cell fusion in response to osmotic disequilibrium. Unlike fps1 mutants, fus1 and fus2 mutants are not influenced by expression of GPD1 or by 1 M sorbitol. Their fusion defect is thus unlikely to result from altered osmotic balance.

scholarly journals Water Transport across Yeast Vacuolar and Plasma Membrane-Targeted Secretory Vesicles Occurs by Passive Diffusion

1999 ◽  
Vol 181 (14) ◽  
pp. 4437-4440 ◽  
Author(s):  
Larry A. Coury ◽  
Mark Hiller ◽  
John C. Mathai ◽  
Elizabeth W. Jones ◽  
Mark L. Zeidel ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Solute Transport ◽  
Water Transport ◽  
Passive Diffusion ◽  
Secretory Vesicles ◽  
Glycerol Facilitator ◽  
Diffusive Flow ◽  
Water Glycerol ◽  
Glycerol Uptake

ABSTRACT To determine whether solute transport across yeast membranes was facilitated, we measured the water and solute permeations of vacuole-derived and late secretory vesicles in Saccharomyces cerevisiae; all permeations were consistent with passive diffusive flow. We also overexpressed Fps1p, the putative glycerol facilitator in S. cerevisiae, in secretory vesicles but observed no effect on water, glycerol, formamide, or urea permeations. However, spheroplasts prepared from the strain overexpressing Fps1p showed enhanced glycerol uptake, suggesting that Fps1p becomes active only upon insertion in the plasma membrane.

scholarly journals Stability of the Glycerol Facilitator in Detergent Solutions†

Biochemistry ◽  
2008 ◽  
Vol 47 (11) ◽  
pp. 3513-3524 ◽  
Author(s):  
Jamie J. Galka ◽  
Simon J. Baturin ◽  
Darren M. Manley ◽  
Angela J. Kehler ◽  
Joe D. O’Neil
Keyword(s):  
Glycerol Facilitator ◽  
Detergent Solutions

scholarly journals The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer

EMBO Reports ◽  
2000 ◽  
Vol 1 (2) ◽  
pp. 183-189 ◽  
Author(s):  
Thomas Braun ◽  
Ansgar Philippsen ◽  
Sabine Wirtz ◽  
Mario J. Borgnia ◽  
Peter Agre ◽  
...  
Keyword(s):  
Glycerol Facilitator

scholarly journals Glycerol Metabolism Is Important for Cytotoxicity of Mycoplasma pneumoniae

2008 ◽  
Vol 191 (3) ◽  
pp. 747-753 ◽  
Author(s):  
Claudine Hames ◽  
Sven Halbedel ◽  
Michael Hoppert ◽  
Joachim Frey ◽  
Jörg Stülke
Keyword(s):  
Hydrogen Peroxide ◽  
Mycoplasma Pneumoniae ◽  
Carbon Sources ◽  
Constitutive Expression ◽  
Glycerol Kinase ◽  
Glycerol Metabolism ◽  
Dihydroxyacetone Phosphate ◽  
Facilitated Diffusion ◽  
Glycolytic Intermediate ◽  
Glycerol Facilitator

ABSTRACT Glycerol is one of the few carbon sources that can be utilized by Mycoplasma pneumoniae. Glycerol metabolism involves uptake by facilitated diffusion, phosphorylation, and the oxidation of glycerol 3-phosphate to dihydroxyacetone phosphate, a glycolytic intermediate. We have analyzed the expression of the genes involved in glycerol metabolism and observed constitutive expression irrespective of the presence of glycerol or preferred carbon sources. Similarly, the enzymatic activity of glycerol kinase is not modulated by HPr-dependent phosphorylation. This lack of regulation is unique among the bacteria for which glycerol metabolism has been studied so far. Two types of enzymes catalyze the oxidation of glycerol 3-phosphate: oxidases and dehydrogenases. Here, we demonstrate that the enzyme encoded by the M. pneumoniae glpD gene is a glycerol 3-phosphate oxidase that forms hydrogen peroxide rather than NADH2. The formation of hydrogen peroxide by GlpD is crucial for cytotoxic effects of M. pneumoniae. A glpD mutant exhibited a significantly reduced formation of hydrogen peroxide and a severely reduced cytotoxicity. Attempts to isolate mutants affected in the genes of glycerol metabolism revealed that only the glpD gene, encoding the glycerol 3-phosphate oxidase, is dispensable. In contrast, the glpF and glpK genes, encoding the glycerol facilitator and the glycerol kinase, respectively, are essential in M. pneumoniae. Thus, the enzymes of glycerol metabolism are crucial for the pathogenicity of M. pneumoniae but also for other essential, yet-to-be-identified functions in the M. pneumoniae cell.

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