A homolog of Ste6p, the a-factor transporter in Saccharomyces cerevisiae, functions bilaterally in Cryptococcus neoformans

碩士 === 國立臺灣大學 === 植物病理學研究所 === 91 === Fungal pheromones have been demonstrated to function in the initial recognition of the fungal mating process. One type of peptide pheromones, identified in the Ascomycetes and Basidiomycetes, terminate in a conserved CAAX motif which triggers sequenti...

Full description

Bibliographic Details
Main Authors: Yen-Ping Hsueh, 薛雁冰
Other Authors: Wei-Chiang Shen
Format: Others
Language:en_US
Published: 2003
Online Access:http://ndltd.ncl.edu.tw/handle/83547066193117256767
id ndltd-TW-091NTU00364009
record_format oai_dc
spelling ndltd-TW-091NTU003640092016-06-20T04:15:30Z http://ndltd.ncl.edu.tw/handle/83547066193117256767 A homolog of Ste6p, the a-factor transporter in Saccharomyces cerevisiae, functions bilaterally in Cryptococcus neoformans 隱球菌費洛蒙傳輸蛋白STE6為其費洛蒙外泌所不可或缺 Yen-Ping Hsueh 薛雁冰 碩士 國立臺灣大學 植物病理學研究所 91 Fungal pheromones have been demonstrated to function in the initial recognition of the fungal mating process. One type of peptide pheromones, identified in the Ascomycetes and Basidiomycetes, terminate in a conserved CAAX motif which triggers sequential post-translational modifications of the pheromone precursors. Among this type of peptide pheromones, a well-studied one is the a-factor of Saccharomyces cerevisiae. The mature a-factor is exported from the cell via an alternative mechanism involving the ATP-binding cassette transporter Ste6p, which is distinct from the typical secretory pathway utilized by most peptides. Unlike the Ascomycetes, the basidiomycetous fungi produce only CAAX motif containing lipopeptide pheromones. Cryptococcus neoformans, a human pathogenic basidiomycetous yeast, causes the life-threatening meningoencephalitis mainly in individuals with compromised immune functions. Virulence studies of the congenic pair of C. neoformans strains have shown that MATa cells are more virulent than MATa cells. Characterization of the mating pheromone genes in the MATa strains suggested an autocrine signaling loop may function and contribute to the virulence of the MATa cells. To further address the role of pheromone in the signaling loop, we have identified STE6 homolog in the C. neoformans genome project at SGTC and begun to dissect its function. By disrupting the STE6, we found that ste6 mutants in either MATa or MATa background showed partially impaired mating function. However, when ste6 MATa and MATa mutants cross with each other, the mating process was completely abolished. Surprisingly, MATa ste6 mutant does not exhibit a defect in haploid fruiting, which implicates that the pheromone molecules could induce the signaling response intracellularly in MATa cells. Our data indicates that the STE6 functions bilaterally and is required for mating but not for haploid fruiting in C. neoformans. Wei-Chiang Shen 沈偉強 2003 學位論文 ; thesis 60 en_US
collection NDLTD
language en_US
format Others
sources NDLTD
description 碩士 === 國立臺灣大學 === 植物病理學研究所 === 91 === Fungal pheromones have been demonstrated to function in the initial recognition of the fungal mating process. One type of peptide pheromones, identified in the Ascomycetes and Basidiomycetes, terminate in a conserved CAAX motif which triggers sequential post-translational modifications of the pheromone precursors. Among this type of peptide pheromones, a well-studied one is the a-factor of Saccharomyces cerevisiae. The mature a-factor is exported from the cell via an alternative mechanism involving the ATP-binding cassette transporter Ste6p, which is distinct from the typical secretory pathway utilized by most peptides. Unlike the Ascomycetes, the basidiomycetous fungi produce only CAAX motif containing lipopeptide pheromones. Cryptococcus neoformans, a human pathogenic basidiomycetous yeast, causes the life-threatening meningoencephalitis mainly in individuals with compromised immune functions. Virulence studies of the congenic pair of C. neoformans strains have shown that MATa cells are more virulent than MATa cells. Characterization of the mating pheromone genes in the MATa strains suggested an autocrine signaling loop may function and contribute to the virulence of the MATa cells. To further address the role of pheromone in the signaling loop, we have identified STE6 homolog in the C. neoformans genome project at SGTC and begun to dissect its function. By disrupting the STE6, we found that ste6 mutants in either MATa or MATa background showed partially impaired mating function. However, when ste6 MATa and MATa mutants cross with each other, the mating process was completely abolished. Surprisingly, MATa ste6 mutant does not exhibit a defect in haploid fruiting, which implicates that the pheromone molecules could induce the signaling response intracellularly in MATa cells. Our data indicates that the STE6 functions bilaterally and is required for mating but not for haploid fruiting in C. neoformans.
author2 Wei-Chiang Shen
author_facet Wei-Chiang Shen
Yen-Ping Hsueh
薛雁冰
author Yen-Ping Hsueh
薛雁冰
spellingShingle Yen-Ping Hsueh
薛雁冰
A homolog of Ste6p, the a-factor transporter in Saccharomyces cerevisiae, functions bilaterally in Cryptococcus neoformans
author_sort Yen-Ping Hsueh
title A homolog of Ste6p, the a-factor transporter in Saccharomyces cerevisiae, functions bilaterally in Cryptococcus neoformans
title_short A homolog of Ste6p, the a-factor transporter in Saccharomyces cerevisiae, functions bilaterally in Cryptococcus neoformans
title_full A homolog of Ste6p, the a-factor transporter in Saccharomyces cerevisiae, functions bilaterally in Cryptococcus neoformans
title_fullStr A homolog of Ste6p, the a-factor transporter in Saccharomyces cerevisiae, functions bilaterally in Cryptococcus neoformans
title_full_unstemmed A homolog of Ste6p, the a-factor transporter in Saccharomyces cerevisiae, functions bilaterally in Cryptococcus neoformans
title_sort homolog of ste6p, the a-factor transporter in saccharomyces cerevisiae, functions bilaterally in cryptococcus neoformans
publishDate 2003
url http://ndltd.ncl.edu.tw/handle/83547066193117256767
work_keys_str_mv AT yenpinghsueh ahomologofste6ptheafactortransporterinsaccharomycescerevisiaefunctionsbilaterallyincryptococcusneoformans
AT xuēyànbīng ahomologofste6ptheafactortransporterinsaccharomycescerevisiaefunctionsbilaterallyincryptococcusneoformans
AT yenpinghsueh yǐnqiújūnfèiluòméngchuánshūdànbáiste6wèiqífèiluòméngwàimìsuǒbùkěhuòquē
AT xuēyànbīng yǐnqiújūnfèiluòméngchuánshūdànbáiste6wèiqífèiluòméngwàimìsuǒbùkěhuòquē
AT yenpinghsueh homologofste6ptheafactortransporterinsaccharomycescerevisiaefunctionsbilaterallyincryptococcusneoformans
AT xuēyànbīng homologofste6ptheafactortransporterinsaccharomycescerevisiaefunctionsbilaterallyincryptococcusneoformans
_version_ 1718310188431179776