Functional analysis of aquaporins Saccharomyces cerevisae

by Nina Pettersson

Publisher: Department of Cell and Molecular Biology, Göteborg University in Göteborg

Written in English
Published: Downloads: 246
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Subjects:

  • Aquaporins,
  • Saccharomyces cerevisiae

Edition Notes

StatementNina Pettersson.
Classifications
LC ClassificationsQP552.A65 P48 2006
The Physical Object
Pagination1 v. (various pagings) :
ID Numbers
Open LibraryOL24000289M
ISBN 109162868063
LC Control Number2006436785

Incipient Balancing Selection through Adaptive Loss of Aquaporins in Natural Saccharomyces cerevisiae Populations. (R = −) and the number of functional aquaporins (R = −) in these strains Genome-wide sequence analysis was performed using unimputed, aligned data from. Bibliography Includes bibliographical references and index. Contents. Structure Function Analysis of Aquaporins and Glycerol Facilitators. Functional Analysis of the Unusual Signature Motifs of the Yeast MIP Channel, Fpslp-- R.M. Bill, et al. GLPF: A Structural Variant of the Aquaporin Tetramer-- T. Braun, et al. Different Behaviours of MIP Proteins in N-Lauroylsarcosine-- L. Duchesne, et al. In Saccharomyces cerevisiae, telomeric DNA is protected by a nonnucleosomal protein complex, tethered by the protein Rap1. Rif and Sir proteins, which interact with Rap1p, are thought to have furth. In a wide range of organisms, dolichyl phosphate mannose (DPM) synthase is a complex of tree proteins Dpm1, Dpm2, and Dpm3. However, in the yeast Saccharomyces cerevisiae, it is believed to be a single Dpm1 protein. The function of Dpm3 is performed in S. cerevisiae by the C-terminal transmembrane domain of the catalytic subunit Dpm1. Until present, the regulatory Dpm2 protein has not been.

Abstract. This chapter covers the functionally characterized plasma membrane carboxylic acids transporters Jen1, Ady2, Fps1 and Pdr12 in the yeast Saccharomyces cerevisiae, addressing also their homologues in other microorganisms, as filamentous fungi and bacteria. Carboxylic acids can either be transported into the cells, to be used as nutrients, or extruded in response to acid stress conditions. Six plasma membrane aquaporins (RsPIPs) and two vacuolar membrane aquaporins (RsTIPs) of radish (Raphanus sativus) were expressed heterologously in Saccharomyces cerevisiae BJ, which is deficient in endogenous functional aquaporin. Aquaporins were detected by immunoblot analysis with corresponding antibodies. A functional aquaporin co-localizes with the vacuolar proton pyrophosphatase to acidocalcisomes and the contractile vacuole complex of Trypanosoma cruzi J Biol Chem. Sep 10;(37) doi: /jbc.M   Methodology/Principal Findings. In this work we propose such a method and apply it in a pilot study of strengths and limitations of Saccharomyces cerevisiae as a model organism. The method relies on the functional classification of proteins into different biological pathways and processes and on full proteome comparisons between the putative model organism and other organisms for which we.

  The genome of the yeast Saccharomyces cerevisiae contains two highly similar classical aquaporin genes, AQY1 and AQY2, and at least two aquaglyceroporins. The diversification into classical aquaporins and aquaglyceroporins is also found in other fungi, such as Dictyostelium, . Purification and functional comparison of nine human Aquaporins produced in Saccharomyces cerevisiae for the purpose of biophysical characterization. Research output: Contribution to journal › Journal article › Research › peer-review. Aquaporins (AQPs) are an ancient family of channel proteins that transport water and neutral solutes through a pore and are found in all eukaryotes and most prokaryotes. A comparison of the amino acid sequences and phylogenetic analysis of 31 full-length cDNAs of maize (Zea mays) AQPs shows that they comprise four different groups of highly divergent proteins. Search Tips. Phrase Searching You can use double quotes to search for a series of words in a particular order. For example, "World war II" (with quotes) will give more precise results than World war II (without quotes). Wildcard Searching If you want to search for multiple variations of a word, you can substitute a special symbol (called a "wildcard") for one or more letters.

Functional analysis of aquaporins Saccharomyces cerevisae by Nina Pettersson Download PDF EPUB FB2

Functional analysis of aquaporins using Saccharomyces cerevisiae Nina Pettersson Medicinaregatan 9C, Box30 Göteborg, Sweden Aquaporins are membrane water channels present in all kinds of organisms, ranging from archaea to human.

In mammals they are distributed in a tissue specific manner and play important roles in body water. Expression of heterologous aquaporins for functional analysis in Saccharomyces cerevisiae. Aquaporins in Saccharomyces cerevisiae wine yeast Jonathan E.

Karpel. Department of Viticulture and Enology, University of California Davis, Davis, CA, Cited by: T1 - Aquaporins in Saccharomyces. T2 - Genetic and functional distinctions between laboratory and wild-type strains. AU - Bonhivers, Mélanie. AU - Carbrey, Jennifer M. AU - Gould, Stephen J.

AU - Agre, Peter. PY - /10/ Y1 - /10/ N2 - Aquaporin water channel proteins mediate the transport of water across cell membranes in numerous Cited by: Expression of heterologous aquaporins for functional analysis in Saccharomyces cerevisiae Article (PDF Available) in Current Genetics 50(4) November with Reads How we measure.

The oligomerization of aquaporins in the yeast Saccharomyces cerevisiae is not understood in detail, but studies with the human erythrocyte aquaporin AQP1 have indicated that the protein is a tetramer composed of functionally independent aqueous pores (Walz et al., ).

Abstract. Our understanding of the functional relevance of orthodox aquaporins and aquaglyceroporins in Saccharomyces cerevisiae is essentially based on phenotypic variations obtained by expression/overexpression/deletion of these major intrinsic proteins in selected strains.

These water/glycerol channels are considered crucial during various life-cycle phases, such as sporulation. Abstract. Aquaporin water channel proteins mediate the transport of water across cell membranes in numerous species.

TheSaccharomyces genome data base contains an open reading frame (here designated AQY1) that encodes a protein with strong homology to 1 from laboratory and wild-type strains of Saccharomyces were expressed inXenopus oocytes to determine the coefficients.

Laizé V Tacnet F Ripoche P and Hohmann S Polymorphism of Saccharomyces cerevisiae aquaporins Yeast in press Google Scholar Rep M Albertyn J Thevelein JM Prior BA and Hohmann S a Different signalling pathways contribute to the control of GPDI gene expression by osmotic stress in Saccharomyces cerevisiae Microbiology   The Saccharomyces cerevisiae genome database contains two ORFs with homology to aquaporins, AQY1 and 1p has been shown to be a functional aquaporin in some strains, such as Σb.

AQY2 is disrupted by a stop codon in most strains; however, Σb has an intact ORF. Because Σb Aqy2p has an intracellular localization in Xenopus oocytes and in yeast, other. Aquaporins in Saccharomyces.

Genetic and functional distinctions between laboratory and wild-type strains. Bonhivers M(1), Carbrey JM, Gould SJ, Agre P. Author information: (1)Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MarylandUSA.

In this study the yeast Saccharomyces cerevisiae, which is a genetically tractable model for analysis of osmoregulation, has been used for analysis of heterologous aquaporins. Aquaporin water channels play important roles in the control of water homeostasis in individual cells and multicellular organisms.

We have investigated the effects of functional expression of the mammalian aquaporins. Expression of heterologous aquaporins for functional analysis in Saccharomyces cerevisiae. Curr. Genet. 50, – /sz [ PubMed ] [ Cross Ref ].

The present study addressed the protective effects against oxidative stress (OS) of a cocoa powder extract (CPEX) on the protein expression profile of S.

cerevisiae. A proteomic analysis was performed after culture preincubation with CPEX either without stress (−OS) or under stress conditions (+OS) (5 mM of H2O2). LC-MS/MS identified 33 differentially expressed proteins (–OS: 14, +OS.

The Saccharomyces cerevisiae strain Sigmab possesses two putative aquaporins, Aqyp and Aqyp. Previous work demonstrated that Aqyp functions as a water channel in Xenopus oocyte.

Pettersson N, Hagström J, Bill RM, Hohmann S () Expression of heterologous aquaporins for functional analysis in Saccharomyces cerevisiae. Curr Genet – PubMed CrossRef Google Scholar Preston GM, Carroll TP, Guggino WB, Agre P () Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.

Pettersson N, Hagstrom J, Bill RM, Hohmann S () Expression of heterologous aquaporins for functional analysis in Saccharomyces cerevisiae.

Curr Genet – CrossRef PubMed Google Scholar Preston GM, Carroll TP, Guggino WB, Agre P () Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Purification and functional comparison of nine human Aquaporins produced in Saccharomyces cerevisiae for the purpose of biophysical characterization Sci Rep.

Dec 4;7(1) doi: /s   Aquaporins mediate rapid selective water transport across biological membranes. Elucidation of their precise physiological roles promises important insight into cellular and organismal osmoregulation.

The genome of the yeast Saccharomyces cerevisiae encodes two similar but differentially regulated aquaporins. Here, we show that expression of AQY1 is stimulated during. Functional analyses have mainly been performed in budding yeast, Saccharomyces cerevisiae, which has two orthodox aquaporins and two aquaglyceroporins.

Whereas Aqy1 is a spore‐specific water channel, Aqy2 is only expressed in proliferating cells and controlled by osmotic signals. Functional analyses are needed to confirm that all the currently identified putative aquaporins have a function in water transport. To date, only the water transport functions of Escherichia coli AqpZ [19] and S.

cerevisiae Aqy1 [15] and Aqy2 [18] have been confirmed experimentally. The yeastSaccharomyces cerevisiaewas used for heterologous expression of the human CHIP28 water Aquaporin-1 channel (Aquaporin-1).A nine-amino-acid epitope of the influenza hemagglutinin protein (HA epitope), recognized by the monoclonal antibody 12CA5, was chosen to tag CHIP28 at its N-terminus.

Alcoholic beverages are produced following the fermentation of sugars by yeasts, mainly (but not exclusively) strains of the species, Saccharomyces cerevisiae.

The sugary starting materials may emanate from cereal starches (which require enzymatic pre-hydrolysis) in the case of beers and whiskies, sucrose-rich plants (molasses or sugar juice from sugarcane) in the case of rums, or from fruits.

In this study the yeast Saccharomyces cerevisiae, which is a genetically tractable model for analysis of osmoregulation, has been used for analysis of heterologous aquaporins.

The yeast Saccharomyces cerevisiae is a widely used and powerful model system in molecular cell biology. Its genome encodes two aquaporins and two aquaglyceroporins (8).

The aquaporins Aqy1 and Aqy2 are 88% identical (excluding the short C terminus) (9–11). However, these proteins seem to be expressed under different conditions: whereas. 1 day ago  Yef3 is an essential protein for the viability of baker’s yeast, Saccharomyces cerevisiae.

It is a member of the ATP-binding cassette F (ABCF) ATPase family, consisting of two ABC-type ATPase domains [17,19]. The paralog of YEF3, HEF3 (homolog of elongation factor 3), arose from an ancient whole-genome duplication event [26,27].

The protease-deficient BJ strain ofSaccharomyces cerevisiae was used in this study. The rat AQP2 mutants L22V, N68S, ND, TM, TM, AT, CW, RC, SP, and PL were generated by PCR-based site-directed mutagenesis.

ND and CW have been shown to be nonfunctional by oocyte expression study. Progress has been made in the heterologous expression of aquaporins; however, it is too early to determine whether the expressed proteins will be suitable for crystallography.

Using a Saccharomyces cerevisiae yeast expression system, Laize et al. were the first to demonstrate moderate to high levels of expression of a recombinant aquaporin.

The. To obtain evidence that PfAQP produced in yeast was active we tested its transport capacity in whole cell assays using the yeast S. cerevisiae, in which systems for testing of aquaporins have been developed.The correct targeting of POpt-PfAQP protein to the membrane was confirmed by Immunoblot on isolated cell membranes, using a polyclonal antibody directed against the protein (Fig.

Isolation and functional analysis of the glycerol permease activity of two new nodulin-like intrinsic the MIP family has been subdivided into two major functional clusters, aquaporins (AQPs) and of the glycerol permease activity of Arabidopsis thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces cerevisiae.

The S. cerevisiae genome contains four MIP homologs ; for two of them, FPS1 and AQY1, functional expression has been demonstrated: FPS1 encodes a glycerol permease while AQY1 is an aquaporin. A deletion mutant of FPS1 shows greatly reduced glycerol uptake activity and was used to characterise the glycerol transport activity of heterologously.Phylogenetic analysis of fungal aquaporins provides insight into their possible role in water transport of mycorrhizal associations Hao Xu, a Janice E.K.

Cooke, b Janusz J. Zwiazek a a Department of Renewable Resources, University of Alberta, Edmonton, AB T6G 2E3, Canada.The absence of a functional AQY1 in some laboratory yeast strains [50, 51] and the absence of a functional AQY2 in most strains [51] may explain why aquaporins present in S.

cerevisiae, unlike.