HwHog1 kinase activity is crucial for survival of Hortaea werneckii in extremely hyperosmolar environments

Kejžar, Anja; Grötli, Morten; Tamás, Markus J.; Plemenitaš, Ana; Lenassi, Metka

doi:10.1016/j.fgb.2014.11.004

Cited by 19 publications

(14 citation statements)

References 57 publications

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“…In a previous study, we showed that the two MAPK paralogs WiHog1A and WiHog1B from W. ichthyophaga differ, as WiHog1A did not complement the function of ScHog1 as efficiently as WiHog1B in S. cerevisiae hog1 Δ cells (Konte and Plemenitaš, 2013 ). This HOG1 -like gene duplication is an unusual trait, which has only been identified in W. sebi (Padamsee et al, 2012 ), H. werneckii (Kejžar et al, 2015 ), Z. rouxii (Iwaki et al, 1999 ), A. nidulans (Furukawa et al, 2005 ), and A. fumigatus (de Oliveira Bruder Nascimento et al, 2016 ). While the paralogous Hog1-like kinases from H. werneckii and Z. rouxii appear to be redundant, in A. nidulans and A. fumigatus their roles are divergent.…”

Section: Discussionmentioning

confidence: 99%

“…Such constitutive phosphorylation patterns of HOG pathway regulation are the reverse to those of yeast and the majority of other fungi, where Hog1 is dephosphorylated under nonstress conditions and phosphorylated upon osmotic shock (Krantz et al, 2006b ; Saito and Posas, 2012 ; Schmidt-Heydt et al, 2013 ). Interestingly, when the cells of halotolerant H. werneckii are grown in up to 3 M NaCl, the phosphorylation patterns are similar to that of S. cerevisiae , but when they are exposed to higher salinities, HwHog1 is phosphorylated constitutively (Kejžar et al, 2015 ). These hybrid phosphorylation patterns might represent the foundations of H. werneckii extreme halotolerance.…”

Section: Discussionmentioning

confidence: 99%

“…The HOG pathway was recently described in detail in halotolerant Hortaea werneckii , where survival of the cells depends on the HOG pathway only at salinities ≥3.0 M NaCl (Kejžar et al, 2015 ). Initial studies of the HOG pathway in W. ichthyophaga showed that its regulation is controlled by rapid dephosphorylation under both hyperosmolar and hypo-osmolar stress (Konte and Plemenitaš, 2013 ).…”

Section: Introductionmentioning

confidence: 99%

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Reconstruction of the High-Osmolarity Glycerol (HOG) Signaling Pathway from the Halophilic Fungus Wallemia ichthyophaga in Saccharomyces cerevisiae

2016

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The basidiomycetous fungus Wallemia ichthyophaga grows between 1.7 and 5.1 M NaCl and is the most halophilic eukaryote described to date. Like other fungi, W. ichthyophaga detects changes in environmental salinity mainly by the evolutionarily conserved high-osmolarity glycerol (HOG) signaling pathway. In Saccharomyces cerevisiae, the HOG pathway has been extensively studied in connection to osmotic regulation, with a valuable knock-out strain collection established. In the present study, we reconstructed the architecture of the HOG pathway of W. ichthyophaga in suitable S. cerevisiae knock-out strains, through heterologous expression of the W. ichthyophaga HOG pathway proteins. Compared to S. cerevisiae, where the Pbs2 (ScPbs2) kinase of the HOG pathway is activated via the SHO1 and SLN1 branches, the interactions between the W. ichthyophaga Pbs2 (WiPbs2) kinase and the W. ichthyophaga SHO1 branch orthologs are not conserved: as well as evidence of poor interactions between the WiSho1 Src-homology 3 (SH3) domain and the WiPbs2 proline-rich motif, the absence of a considerable part of the osmosensing apparatus in the genome of W. ichthyophaga suggests that the SHO1 branch components are not involved in HOG signaling in this halophilic fungus. In contrast, the conserved activation of WiPbs2 by the S. cerevisiae ScSsk2/ScSsk22 kinase and the sensitivity of W. ichthyophaga cells to fludioxonil, emphasize the significance of two-component (SLN1-like) signaling via Group III histidine kinase. Combined with protein modeling data, our study reveals conserved and non-conserved protein interactions in the HOG signaling pathway of W. ichthyophaga and therefore significantly improves the knowledge of hyperosmotic signal processing in this halophilic fungus.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Reconstruction of the High-Osmolarity Glycerol (HOG) Signaling Pathway from the Halophilic Fungus Wallemia ichthyophaga in Saccharomyces cerevisiae

2016

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“…For example, in Candida albicans , the Sho1-Ste11 branch does not relay osmotic stress signals to Hog1. This is mediated solely by the Ssk2 MAPKKK, which is regulated by both Sln1 dependent and independent mechanisms 16 , while the extremely halotolerant Hortaea werneckii has two redundant Hog1 homologues 17 . Moreover, in the model yeast Schizosaccharomyces pombe , there is no Sln1 homologue and instead distinct histidine kinases relay oxidative and not osmotic stress signals to the Hog1 homologue Sty1/Spc1 18 .…”

Section: Introductionmentioning

confidence: 99%

Influence of ylHog1 MAPK kinase on Yarrowia lipolytica stress response and erythritol production

Rzechonek

Day

Quinn

et al. 2018

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Erythritol production is a unique response to hyperosmotic stress that is observed in a small group of yeasts, including Yarrowia lipolytica. This study investigated whether this unusual mechanism is regulated by the HOG pathway, well described in Saccharomyces cerevisiae. The gene YALI0E25135g was identified as the Y. lipolytica homologue of HOG1 and was found to be phosphorylated in response to hyperosmotic shock. Deletion of the gene caused a significant decrease in resistance to hyperosmotic stress and negatively affected erythritol production. Interestingly, the deletion strain yl-hog1Δ displayed significant morphological defects, with the cells growing in a filamentous form. Moreover, yl-hog1Δ cells were also resistant to the cell wall damaging agents Congo red and calcofluor white. Collectively, these results indicate that yl-Hog1 is crucial for the cellular response to hyperosmotic stress, plays a role in the induction of erythritol production, and potentially prevents cross-talk with different MAPK signalling pathways in the cell.

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“…Having virtually the same size and being 69% identical, W. ichthyophaga WiHog1A and WiHog1B genes are differentially induced by high osmolarity and show different degrees of complementation of a S. cerevisiae Δhog1 mutant ( Konte and Plemenitas, 2013 ). With evidence supporting an ancestral duplication of its entire genome, H. werneckii contains the two nearly identical (95%) and functionally redundant SAPKs HwHog1A and HwHog1B, which show osmolyte-type-dependent phosphorylation ( Kejzar et al, 2015 ).…”

Section: Introductionmentioning

confidence: 99%

SakA and MpkC Stress MAPKs Show Opposite and Common Functions During Stress Responses and Development in Aspergillus nidulans

et al. 2018

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Stress activated MAP kinases (SAPKs) of the Hog1/Sty1/p38 family are specialized in transducing stress signals. In contrast to what is seen in animal cells, very few fungal species contain more than one SAPK. Aspergillus nidulans and other Aspergilli contain two SAPKs called SakA/HogA and MpkC. We have shown that SakA is essential for conidia to maintain their viability and to survive high H2O2 concentrations. H2O2 induces SakA nuclear accumulation and its interaction with transcription factor AtfA. Although SakA and MpkC show physical interaction, little is known about MpkC functions. Here we show that ΔmpkC mutants are not sensitive to oxidative stress but in fact MpkC inactivation partially restores the oxidative stress resistance of ΔsakA mutants. ΔmpkC mutants display about twofold increase in the production of fully viable conidia. The inactivation of the SakA upstream MAPKK PbsB or the simultaneous elimination of sakA and mpkC result in virtually identical phenotypes, including decreased radial growth, a drastic reduction of conidiation and a sharp, progressive loss of conidial viability. SakA and to a minor extent MpkC also regulate cell-wall integrity. Given the roles of MpkC in conidiation and oxidative stress sensitivity, we used a functional MpkC::GFP fusion to determine MpkC nuclear localization as an in vivo indicator of MpkC activation during asexual development and stress. MpkC is mostly localized in the cytoplasm of intact conidia, accumulates in nuclei during the first 2 h of germination and then becomes progressively excluded from nuclei in growing hyphae. In the conidiophore, MpkC nuclear accumulation increases in vesicles, metulae and phialides and decreases in older conidia. Oxidative and osmotic stresses induce MpkC nuclear accumulation in both germinating conidia and hyphae. In all these cases, MpkC nuclear accumulation is largely dependent on the MAPKK PbsB. Our results indicate that SakA and MpkC play major, distinct and sometimes opposing roles in conidiation and conidiospore physiology, as well as common roles in response to stress. We propose that two SAPKs are necessary to delay (MpkC) or fully stop (SakA) mitosis during conidiogenesis and the terminal differentiation of conidia, in the highly prolific phialoconidiation process characteristic of the Aspergilli.

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HwHog1 kinase activity is crucial for survival of Hortaea werneckii in extremely hyperosmolar environments

Cited by 19 publications

References 57 publications

Reconstruction of the High-Osmolarity Glycerol (HOG) Signaling Pathway from the Halophilic Fungus Wallemia ichthyophaga in Saccharomyces cerevisiae

Reconstruction of the High-Osmolarity Glycerol (HOG) Signaling Pathway from the Halophilic Fungus Wallemia ichthyophaga in Saccharomyces cerevisiae

Influence of ylHog1 MAPK kinase on Yarrowia lipolytica stress response and erythritol production

SakA and MpkC Stress MAPKs Show Opposite and Common Functions During Stress Responses and Development in Aspergillus nidulans

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