The hypo-osmolarity-sensitive phenotype of the Saccharomyces cerevisiae hpo2 mutant is due to a mutation in PKC1, which regulates expression of β-glucanase

Shimizu, Jiro; Yoda, Koji; Yamasaki, Makari

doi:10.1007/bf00283417

Cited by 61 publications

(67 citation statements)

References 32 publications

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“…For us, the most interesting one is the connection of MKC1 function to growth control and its influence on the generation of a stable wall structure. Some of the mechanisms that relate the function of the Pkc1p-controlled cascade with enzymes that can be relevant in the generation of the cell wall in S. cerevisiae are beginning to emerge (62). The discovery of conditions that kill the mkc1⌬/mkc1⌬ strain, such as high concentrations of calcium or caffeine, should enable us to look for suppressors of this lethal phenotype with the use of a genetic transformation system developed in our laboratory (54).…”

Section: Discussionmentioning

confidence: 99%

Functional Characterization of the MKC1 Gene of Candida albicans, Which Encodes a Mitogen-Activated Protein Kinase Homolog Related to Cell Integrity

Navarro‐García

Sánchez

Pla

et al. 1995

Molecular and Cellular Biology

183

154

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Mitogen-activated protein (MAP) kinases represent a group of serine/threonine protein kinases playing a central role in signal transduction processes in eukaryotic cells. Using a strategy based on the complementation of the thermosensitive autolytic phenotype of slt2 null mutants, we have isolated a Candida albicans homolog of Saccharomyces cerevisiae MAP kinase gene SLT2 (MPK1), which is involved in the recently outlined PKC1-controlled signalling pathway. The isolated gene, named MKC1 (MAP kinase from C. albicans), coded for a putative protein, Mkc1p, of 58,320 Da that displayed all the characteristic domains of MAP kinases and was 55% identical to S. cerevisiae Slt2p (Mpk1p). The MKC1 gene was deleted in a diploid Candida strain, and heterozygous and homozygous strains, in both Ura ؉ and Ura ؊ backgrounds, were obtained to facilitate the analysis of the function of the gene. Deletion of the two alleles of the MKC1 gene gave rise to viable cells that grew at 28 and 37؇C but, nevertheless, displayed a variety of phenotypic traits under more stringent conditions. These included a low growth yield and a loss of viability in cultures grown at 42؇C, a high sensitivity to thermal shocks at 55؇C, an enhanced susceptibility to caffeine that was osmotically remediable, and the formation of a weak cell wall with a very low resistance to complex lytic enzyme preparations. The analysis of the functions downstream of the MKC1 gene should contribute to understanding of the connection of growth and morphogenesis in pathogenic fungi.

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Section: Discussionmentioning

confidence: 99%

Functional Characterization of the MKC1 Gene of Candida albicans, Which Encodes a Mitogen-Activated Protein Kinase Homolog Related to Cell Integrity

Navarro‐García

Sánchez

Pla

et al. 1995

Molecular and Cellular Biology

183

154

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“…Both the inner, glucan-containing layer and the outer, mannoprotein layer are thinner in pkc1D mutants. These alterations are mirrored by a reduction in both b-1,3-and b-1,6-glucans of 30% and a reduction in mannan of 20% (Roemer et al 1994;Shimizu et al 1994). Loss of PKC1 results in a more severe growth defect than that displayed by deletion of any of the members of the MAPK cascade under the control of Pkc1, which prompted the suggestion that Pkc1 regulates at least one additional pathway (Lee and Levin 1992).…”

Section: Pkc1 and The Cwi Mapk Cascadementioning

confidence: 99%

Regulation of Cell Wall Biogenesis in Saccharomyces cerevisiae: The Cell Wall Integrity Signaling Pathway

2011

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The yeast cell wall is a strong, but elastic, structure that is essential not only for the maintenance of cell shape and integrity, but also for progression through the cell cycle. During growth and morphogenesis, and in response to environmental challenges, the cell wall is remodeled in a highly regulated and polarized manner, a process that is principally under the control of the cell wall integrity (CWI) signaling pathway. This pathway transmits wall stress signals from the cell surface to the Rho1 GTPase, which mobilizes a physiologic response through a variety of effectors. Activation of CWI signaling regulates the production of various carbohydrate polymers of the cell wall, as well as their polarized delivery to the site of cell wall remodeling. This review article centers on CWI signaling in Saccharomyces cerevisiae through the cell cycle and in response to cell wall stress. The interface of this signaling pathway with other pathways that contribute to the maintenance of cell wall integrity is also discussed.

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“…6C). Various mutants with a defective cell wall biosynthesis or N-glycosylation were reported to reveal an SDS sensitivity (63,64). The different behavior of ⌬ost6 and ⌬ost3 null mutants toward these compounds could mean that both genes may in part be involved in different functions important for cell wall biogenesis and/or stability.…”

Section: Ost3 and Ost6 Are Required For N-glycosylation In Vivo And mentioning

confidence: 99%

The Oligosaccharyltransferase Complex from Saccharomyces cerevisiae

Knauer

Lehle

1999

Journal of Biological Chemistry

112

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The key step of N-glycosylation of proteins, an essential and highly conserved protein modification, is catalyzed by the hetero-oligomeric protein complex oligosaccharyltransferase (OST). So far, eight genes have been identified in Saccharomyces cerevisiae that are involved in this process. Enzymatically active OST preparations from yeast were shown to be composed of four (Ost1p, Wbp1p, Ost3p, Swp1p) or six subunits (Ost2p and Ost5p in addition to the four listed). Genetic studies have disclosed Stt3p and Ost4p as additional proteins needed for N-glycosylation. In this study we report the identification and functional characterization of a new OST gene, designated OST6, that has homology to OST3 and in particular a strikingly similar membrane topology. Neither gene is essential for growth of yeast. Disruption of OST6 or OST3 causes only a minor defect in N-glycosylation, but an ⌬ost3⌬ost6 double mutant displays a synthetic phenotype, leading to a severe underglycosylation of soluble and membrane-bound glycoproteins in vivo and to a reduced OST activity in vitro. Moreover, each of the two genes has also a specific function, since agents affecting cell wall biogenesis reveal different growth phenotypes in the respective null mutants. By blue native electrophoresis and immunodetection, a ϳ240-kDa complex was identified consisting of Ost1p, Stt3p, Wbp1p, Ost3p, Ost6p, Swp1p, Ost2p, and Ost5p, indicating that probably all so far identified OST proteins are constituents of the OST complex. It is also shown that disruption of OST3 and OST6 leads to a defect in the assembly of the complex. Hence, the function of these genes seems to be essential for recruiting a fully active complex necessary for efficient N-glycosylation.

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The hypo-osmolarity-sensitive phenotype of the Saccharomyces cerevisiae hpo2 mutant is due to a mutation in PKC1, which regulates expression of β-glucanase

Cited by 61 publications

References 32 publications

Functional Characterization of the MKC1 Gene of Candida albicans, Which Encodes a Mitogen-Activated Protein Kinase Homolog Related to Cell Integrity

Functional Characterization of the MKC1 Gene of Candida albicans, Which Encodes a Mitogen-Activated Protein Kinase Homolog Related to Cell Integrity

Regulation of Cell Wall Biogenesis in Saccharomyces cerevisiae: The Cell Wall Integrity Signaling Pathway

The Oligosaccharyltransferase Complex from Saccharomyces cerevisiae

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