Isolation and sequence of theHOG1 homologue fromDebaryomyces hansenii by complementation of thehog1? strain ofSaccharomyces cerevisiae

Bansal, Parmil K.; Mondal, Alok K.

doi:10.1002/(sici)1097-0061(20000115)16:1<81::aid-yea510>3.0.co;2-i

Cited by 55 publications

(37 citation statements)

References 32 publications

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“…In addition, genes encoding homologs of YPD1 (80) and SSK1 (78, 81) have been described in C. albicans. Furthermore, HOG1 genes have been isolated from the osmotolerant yeast Zygosaccharomyces rouxii (250,285) and the salt-tolerant yeast Debaryomyces hansenii (26). SHO1 homologs have been reported from Candida utilis and Kluyveromyces lactis (554).…”

Section: Osmosensing Signaling Pathways In Other Yeastsmentioning

confidence: 99%

Osmotic Stress Signaling and Osmoadaptation in Yeasts

Hohmann

2002

Microbiol Mol Biol Rev

1,526

1,440

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The ability to adapt to altered availability of free water is a fundamental property of living cells. The principles underlying osmoadaptation are well conserved. The yeast Saccharomyces cerevisiae is an excellent model system with which to study the molecular biology and physiology of osmoadaptation. Upon a shift to high osmolarity, yeast cells rapidly stimulate a mitogen-activated protein (MAP) kinase cascade, the high-osmolarity glycerol (HOG) pathway, which orchestrates part of the transcriptional response. The dynamic operation of the HOG pathway has been well studied, and similar osmosensing pathways exist in other eukaryotes. Protein kinase A, which seems to mediate a response to diverse stress conditions, is also involved in the transcriptional response program. Expression changes after a shift to high osmolarity aim at adjusting metabolism and the production of cellular protectants. Accumulation of the osmolyte glycerol, which is also controlled by altering transmembrane glycerol transport, is of central importance. Upon a shift from high to low osmolarity, yeast cells stimulate a different MAP kinase cascade, the cell integrity pathway. The transcriptional program upon hypo-osmotic shock seems to aim at adjusting cell surface properties. Rapid export of glycerol is an important event in adaptation to low osmolarity. Osmoadaptation, adjustment of cell surface properties, and the control of cell morphogenesis, growth, and proliferation are highly coordinated processes. The Skn7p response regulator may be involved in coordinating these events. An integrated understanding of osmoadaptation requires not only knowledge of the function of many uncharacterized genes but also further insight into the time line of events, their interdependence, their dynamics, and their spatial organization as well as the importance of subtle effects

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Section: Osmosensing Signaling Pathways In Other Yeastsmentioning

confidence: 99%

Osmotic Stress Signaling and Osmoadaptation in Yeasts

Hohmann

2002

Microbiol Mol Biol Rev

1,526

1,440

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“…MAPKs homologous to S. cerevisiae Hog1p have been identified in different yeast species such as Schizosaccharomyces pombe (46), Candida albicans (57), Z. rouxii (37), and D. hansenii (9) as well as in multicellular fungi including Aspergillus nidulans (31), Neurospora crassa (70), and the human pathogen Cryptococcus neoformans (8). Although only a few of them have been studied in detail, it appears that Hog1p orthologues share conserved but different roles in response to a variety of environmental cues.…”

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confidence: 99%

Hog1 Mitogen-Activated Protein Kinase Plays Conserved and Distinct Roles in the Osmotolerant Yeast Torulaspora delbrueckii

2006

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Torulaspora delbrueckii has emerged during evolution as one of the most osmotolerant yeasts. However, the molecular mechanisms underlying this unusual stress resistance are poorly understood. In this study, we have characterized the functional role of the high-osmolarity glycerol (HOG) mitogen-activated protein kinase pathway in mediating the osmotic stress response, among others, in T. delbrueckii. We show that the T. delbrueckii Hog1p homologue TdHog1p is phosphorylated after cell transfer to NaCl-or sorbitol-containing medium. However, TdHog1p plays a minor role in tolerance to conditions of moderate osmotic stress, a trait related mainly with the osmotic balance. In consonance with this, the absence of TdHog1p produced only a weak defect in the timing of the osmostress-induced glycerol and GPD1 mRNA overaccumulation. Tdhog1⌬ mutants also failed to display aberrant morphology changes in response to osmotic stress. Furthermore, our data indicate that the T. delbrueckii HOG pathway has evolved to respond to specific environmental conditions and to play a pivotal role in the stress cross-protection mechanism.

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“…For cloning of DPBS2 gene, a genomic library of D. hansenii constructed previously in our laboratory (Bansal and Mondal, 2000) was used. A total of 3 mg plasmid library was used to transform S. cerevisiae strain PB29 by the lithium acetate method (Geitz and Schiestl, 1995).…”

Section: Cloning Of the Dpbs2 Genementioning

confidence: 99%

“…The characterization of such genes could therefore provide insight into its complex physiological role. Recently, an osmosensing MAP kinase pathway has been shown to be present in the yeast Debaryomyces hansenii (Bansal and Mondal, 2000). This species is considered to be a very highly halotolerant yeast, as it is capable of growing in media containing 4 M NaCl (Adler et al, 1985;Norkrans, 1966;Onishi, 1963).…”

Section: Introductionmentioning

confidence: 99%

A PBS2 homologue from Debaryomyces hansenii shows a differential effect on calcofluor and polymyxin B sensitivity in Saccharomyces cerevisiae

Bansal

Sharma

Mondal

2001

Yeast

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The PBS2 gene encodes a MAP kinase kinase that plays a pivotal role in osmosensing signal-transduction pathway in the yeast Saccharomyces cerevisiae. Mutation in the PBS2 gene has a pleotropic effect. Besides being osmosensitive, pbs2 mutants show altered sensitivity to polymyxin B and calcofluor. Recent studies revealed that Pbs2p plays a different role in osmoadaptation and calcofluor sensitivity. We have isolated a gene homologous to PBS2 from the highly salt-tolerant yeast Debaryomyces hansenii by phenotypic complementation. DNA sequencing of the clone revealed that the gene encoded a protein of 683 amino acid residues. Like Pbs2p, this protein also has a proline-rich motif. Further characterization revealed that this gene could complement polymyxin B sensitivity but did not affect calcofluor sensitivity. Thus, it appeared that Pbs2p also has an independent role in these two physiological processes. The

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Isolation and sequence of theHOG1 homologue fromDebaryomyces hansenii by complementation of thehog1? strain ofSaccharomyces cerevisiae

Cited by 55 publications

References 32 publications

Osmotic Stress Signaling and Osmoadaptation in Yeasts

Osmotic Stress Signaling and Osmoadaptation in Yeasts

Hog1 Mitogen-Activated Protein Kinase Plays Conserved and Distinct Roles in the Osmotolerant Yeast Torulaspora delbrueckii

A PBS2 homologue from Debaryomyces hansenii shows a differential effect on calcofluor and polymyxin B sensitivity in Saccharomyces cerevisiae

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