Eukaryotic Cell Journal Impact Factor & Information

Publisher: American Society for Microbiology, American Society for Microbiology

Journal description

Eukaryotic Cell (EC) focuses on eukaryotic microbiology and presents reports of basic research on simple eukaryotic microorganisms such as yeasts, fungi, algae, protozoa, and social amoebae. The journal also covers viruses of these organisms and their organelles and their interactions with other living systems, where the focus is on the eukaryotic cell.

Current impact factor: 3.18

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 3.179
2012 Impact Factor 3.586
2011 Impact Factor 3.604
2010 Impact Factor 3.395
2009 Impact Factor 3.806
2008 Impact Factor 3.83
2007 Impact Factor 3.399
2006 Impact Factor 3.707
2005 Impact Factor 4.303
2004 Impact Factor 3.954
2003 Impact Factor 3.267

Impact factor over time

Impact factor

Additional details

5-year impact 3.77
Cited half-life 5.40
Immediacy index 0.65
Eigenfactor 0.02
Article influence 1.32
Website Eukaryotic Cell website
Other titles Eukaryotic cell (Online), Eukaryotic cell
ISSN 1535-9786
OCLC 47259667
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

American Society for Microbiology

  • Pre-print
    • Author cannot archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Cannot archive before publication
    • Author's version
    • Author's post-print on funder's repositories, institutional repository or subject-based repositories
    • Non-commercial
    • Publisher's version/PDF may be used
    • Publisher's version/PDF may be used on author's personal website or employers website
    • Recommended that author's post-prints submitted to PubMed or institutional repositories are made available 6 months after publication
    • Reviewed on 30th June 2014
  • Classification
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Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Polarized growth in filamentous fungi needs a continuous supply of proteins and lipids to the growing hyphal tip. One of the important membrane compounds in fungi is ergosterol. At the apical plasma membrane ergosterol accumulations, which are called sterol-rich plasma membrane domains (SRDs). The exact roles and formation mechanism of the SRDs remained unclear, although the importance has been recognized for hyphal growth. Transport of ergosterol to hyphal tips is thought to be important for the organization of the SRDs. Oxysterol binding proteins, which are conserved from yeast to human, are involved in non-vesicular sterol transport. In Saccharomyces cerevisiae seven oxysterol-binding proteins homologues (OSH1-7) play a role in ergosterol distribution between closely located membranes independent of vesicle transport. We found five homologous genes (oshA-E) in the filamentous fungi Aspergillus nidulans. The functions of OshA-E were characterized by gene deletion and subcellular localization. Each gene-deletion strain showed characteristic phenotypes and different sensitivities to ergosterol-associated drugs. GFP tagged Osh proteins showed specific localization at late Golgi, puncta associated with the ER, or diffusely in the cytoplasm. The genes expression and regulation were investigated in a medically important species Aspergillus fumigatus as well as A. nidulans. Our results suggest that each Osh protein plays a role in ergosterol distribution at distinct sites and contributes to proper fungal growth. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 06/2015; DOI:10.1128/EC.00027-15
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    ABSTRACT: Filamentous growth is a microbial differentiation response that involves the concerted action of multiple signaling pathways. In budding yeast, one pathway that regulates filamentous growth is a Cdc42p-dependent mitogen activated protein kinase (MAPK) pathway. Several transmembrane (TM) proteins regulate the filamentous growth pathway, including the signaling mucin, Msb2p, the tetraspan osmosensor, Sho1p, and an adaptor, Opy2p. The TM proteins were compared to identify common and unique features. Msb2p, Sho1p, and Opy2p associated by co-immunoprecipitation analysis but showed predominately different localization patterns. The different localization patterns of the proteins resulted, in part, from different rates of turnover from the PM. In particular, Msb2p (and Opy2p) were turned over rapidly compared to Sho1p. Msb2p signaled from the PM and its turnover was a rate-limiting step in MAPK signaling. Genetic analysis identified unique phenotypes of cells overexpressing the TM proteins. Therefore, each TM regulator of the filamentous growth pathway has a unique regulatory pattern and specific function in regulating filamentous growth. This specialization may be important for fine-tuning and potentially diversifying the filamentation response. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 06/2015; DOI:10.1128/EC.00085-15
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    ABSTRACT: Very high ethanol tolerance is a distinctive trait of the yeast Saccharomyces cerevisiae, with notable ecological and industrial importance. Although many genes have been shown to be required for moderate ethanol tolerance (i.e. 6 to 12%) in laboratory strains, little is known for the much higher ethanol tolerance (i.e. 16 to 20%) in natural and industrial strains. We have analysed the genetic basis of very high ethanol tolerance in a Brazilian bio-ethanol production strain by genetic mapping with laboratory strains containing artificially inserted oligonucleotide markers. The first locus contained the ura3Δ0 mutation of the lab strain as the causative mutation. Analysis of other auxotrophies also revealed significant linkage for LYS2, LEU2, HIS3 and MET15. Only tolerance to very high ethanol concentrations was reduced by auxotrophies, while the effect was reversed at lower concentrations. Evaluation of other stress conditions showed that the link with auxotrophy is dependent on the type of stress condition and the type of auxotrophy. When the concentration of the auxotrophic nutrient is close to that limiting growth, more stress conditions can inhibit growth of an auxotrophic strain. We show that very high ethanol concentrations inhibit the uptake of leucine more than that of uracil, but the 500-fold lower uracil uptake activity may explain the stronger linkage between uracil auxotrophy and ethanol sensitivity compared to leucine auxotrophy. Since very high concentrations of ethanol inhibit uptake of auxotrophic nutrients, the active uptake of scarce nutrients may be a major limiting factor for growth under ethanol stress. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 06/2015; DOI:10.1128/EC.00053-15
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    ABSTRACT: The centriole in eukaryotes functions as the cell's microtubule-organizing center (MTOC) to nucleate spindle assembly, and its biogenesis requires an evolutionarily conserved protein, SAS-6, which assembles the centriole cartwheel. Trypanosoma brucei, an early branching protozoan, possesses the basal body as its MTOC to nucleate flagellum biogenesis. However, little is known about the components of the basal body and their roles in basal body biogenesis and flagellum assembly. Here we report that the T. brucei SAS-6 homolog, TbSAS-6, is localized to the mature basal body and the pro-basal body throughout the cell cycle. RNAi of TbSAS-6 inhibited pro-basal body biogenesis, compromised flagellum assembly, and caused cytokinesis arrest. Surprisingly, overexpression of TbSAS-6 in T. brucei also impaired pro-basal body duplication and flagellum assembly, contrary to SAS-6 overexpression in humans which produces supernumerary centrioles. Furthermore, we showed that depletion of Polo-like kinase, TbPLK, or inhibition of TbPLK activity did not abolish TbSAS-6 localization to the basal body, in contrast to the essential role of Polo-like kinase in recruiting SAS-6 to centrioles in animals. Altogether, these results identified the essential role of TbSAS-6 in pro-basal body biogenesis and flagellum assembly, and suggest the presence of a TbPLK-independent pathway governing basal body duplication in T. brucei. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 06/2015; DOI:10.1128/EC.00083-15
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    ABSTRACT: In many organisms, sophisticated mechanisms facilitate release of peptides in response to extracellular stimuli. In the ciliate Tetrahymena thermophila, efficient peptide secretion depends on specialized vesicles called mucocysts that contain dense crystalline cores that expand rapidly during exocytosis. Core assembly depends of endoproteolytic cleavage of mucocyst proproteins by an aspartyl protease, Cathepsin 3 (CTH3). Here, we show that a second enzyme identified by expression profiling, Cth4p, is also required for processing of proGrl proteins and for assembly of functional mucocysts. Cth4p is a cysteine cathepsin that localizes partially to endolysosomal structures, and appears to act downstream of, and may be activated by, Cth3p. Disruption of CTH4 results in cells (Δcth4) that show aberrant trimming of Grl proproteins, as well as grossly aberrant mucocyst exocytosis. Surprisingly, Δcth4 cells succeed in assembling crystalline mucocyst cores. However, those cores do not undergo normal directional expansion during exocytosis, and thus fail to efficiently extrude from the cells. We could phenocopy the Δcth4 defects by mutating conserved catalytic residues, indicating that the in vivo function of Cth4p is enzymatic. Our results indicate that, as for canonical proteins packaged in animal secretory granules, the maturation of mucocyst proproteins involves sequential processing steps. The Δcth4 defects uncouple, in an unanticipated way, the assembly of mucocyst cores and their subsequent expansion, and thereby reveals a previously unsuspected aspect of polypeptide secretion in ciliates. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 06/2015; DOI:10.1128/EC.00058-15
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    ABSTRACT: The gametogenesis program of the budding yeast Saccharomyces cerevisiae, also known as sporulation, employs an unusual internal meiotic division, following which all four meiotic products differentiate within the parental cell. We showed previously that sporulation is typically accompanied by the destruction of discarded immature meiotic products through their exposure to proteases released from the mother cell vacuole, which undergoes an apparent programmed rupture. Here we demonstrate that vacuolar rupture contributes to a de facto programmed cell death (PCD) of the meiotic mother cell itself. Meiotic mother PCD is accompanied by an accumulation of depolarized mitochondria, organelle swelling, altered plasma membrane characteristics, and cytoplasmic clearance. To ensure that the gametes survive the destructive consequences of developing within a cell that is executing PCD, we hypothesized that PCD is restrained from occurring until spores have attained a threshold degree of differentiation. Consistent with this hypothesis, gene deletions that perturb all but the most terminal post-meiotic spore developmental stages are associated with altered PCD. In these mutants, meiotic mother cells exhibit a delay in vacuolar rupture, and then appear to undergo an alternative form of PCD associated with catastrophic consequences for the under-developed spores. Our findings reveal yeast sporulation as a context of bona fide PCD that is developmentally coordinated with gamete differentiation. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 06/2015; DOI:10.1128/EC.00068-15
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    ABSTRACT: Candida glabrata is reported as the second most prevalent human opportunistic fungal pathogen in the United States. Over the last decades its incidence increased whereas that of C. albicans decreased slightly. One of the main reasons for this shift is attributed to the inherent tolerance of C. glabrata towards the commonly used azole antifungal drugs. Despite a close phylogenetic distance with Saccharomyces cerevisiae, homologous recombination works with poor efficiency in C. glabrata, as compared to baker's yeast, in fact limiting targeted genetic alterations of the pathogen's genome.. It has been shown that non-homologous DNA end joining is dominant over specific gene targeting in C. glabrata. To improve the homologous recombination efficiency we have generated a strain deleted for the LIG4 gene, which resulted in a significant increase in correct gene targeting. The very specific function of Lig4 in mediating non-homologous end joining is the reason for the absence of clear side effects, some of which affect the ku80 mutant, another mutant with reduced non-homologous end joining. We also generated a LIG4 re-integration cassette. Our results show that the lig4 mutant strain may be a valuable tool for the C. glabrata community. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 06/2015; DOI:10.1128/EC.00281-14
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    ABSTRACT: A biochemical pathway for the incorporation of cell wall protein into the cell wall of Neurospora crassa has recently been proposed. In this pathway, the DFG-5 and DCW-1 endo-α-1,6-mannanases function to covalently cross-link cell wall protein-associated N-linked galactomannans, which are structurally related to the yeast outer chain mannans, into the cell wall glucan-chitin matrix. In this report we demonstrate that the mannosyltransferase enzyme Och1p, which is needed for the synthesis of the N-linked outer chain mannan, is essential for the incorporation of cell wall glycoprotein into the Candida albicans cell wall. Using endoglycosidases, we show that C. albicans cell wall proteins are cross-linked into the cell wall via their N-linked outer chain mannans. We further demonstrate that the Dfg5p and Dcw1p α-1,6-mannanases are needed for the incorporation of cell wall glycoproteins into the C. albicans cell wall. Our results support the hypothesis that the Dfg5p and Dcw1p α-1,6-mannanases incorporate cell wall glycoproteins into the C. albicans cell wall by cross-linking outer chain mannans into the cell wall glucan/chitin matrix. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 06/2015; DOI:10.1128/EC.00032-15
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    ABSTRACT: Microbial secretion is integral for regulating cell homeostasis as well as releasing virulence factors during infection. Phosphatidylserine synthase (CHO1) and phosphatidylserine decarboxylase (PSD1 and PSD2) are Candida albicans genes involved in phospholipid biosynthesis, and mutations in these genes affect mitochondrial function, cell wall thickness, and virulence in mice. We tested the role of these genes in several agar-based secretion assays and observed that the cho1Δ/Δ and psd1Δ/Δ psd2Δ/Δ strains manifested less protease and phospholipase activity. Since extracellular vesicles (EVs) are surrounded by a lipid membrane, we investigated the effects of these mutations on EV structure, composition, and biological activity. The cho1Δ/Δ mutant releases EVs comparable in size to wild-type EVs, but EVs from the psd1Δ/Δ psd2Δ/Δ strain are much larger than those from the wild-type, including a population of >100 nm EVs not observed in the EVs from wild type. Proteomic analysis revealed that EVs from both mutants had significantly different protein cargo than those from wild-type. EVs were tested for their ability to activate NFkB in bone marrow-derived macrophage cells. While wild-type and psd1Δ/Δ psd2Δ/Δ mutant-derived EVs activated NFkB, the cho1Δ/Δ mutant-derived EV did not. These studies indicate that the presence and absence of these C. albicans genes have qualitative and quantitative effects on EV size, composition, and immunostimulatory phenotypes that highlight a complex interplay between lipid metabolism and vesicle production. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 05/2015; DOI:10.1128/EC.00054-15
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    ABSTRACT: Candida albicans is a major fungal pathogen whose virulence is associated with its ability to transition from a budding yeast form to invasive hyphal filaments. The kinesin-14 family member CaKar3 is required for transition between these morphological states, as well as for mitotic progression and karyogamy. While kinesin-14s are ubiquitous, CaKar3 homologs in Hemiascomycete fungi are unique as they form heterodimers with non-catalytic kinesin-like proteins. Thus, CaKar3-based motors may represent a novel antifungal drug target. We have identified and examined the roles of a kinesin-like regulator of CaKar3. We show that orf19.306 (dubbed CaCIK1) encodes a protein that forms a heterodimer with CaKar3, localizes CaKar3 to spindle pole bodies, and can bind microtubules and influence CaKar3 mechanochemistry despite lacking ATPase activity of its own. Similar to CaKar3 depletion, loss of CaCik1 results in cell cycle arrest, filamentation defects, and an inability to undergo karyogamy. Furthermore, examination of spindle structure in cells lacking either of these proteins shows that a large proportion have a monopolar spindle or two dissociated half-spindles; a phenotype unique to the C. albicans kinesin-14 homolog. These findings provide new insights mitotic spindle structure and kinesin motor function in C. albicans, and identify a potentially vulnerable target for antifungal drug development. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 05/2015; DOI:10.1128/EC.00015-15
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    ABSTRACT: The plasma membrane aquaglyceroporin Fps1 is responsible for glycerol transport in yeast in response to changes in extracellular osmolarity. Fps1 functions as a homotetramer and control of its channel activity in response to hyper-osmotic shock involves a redundant pair of fungal-specific regulators, Rgc1 and Rgc2 (regulators of the glycerol channel), and the MAPK Hog1 (high osmolarity glycerol response). Rgc1 and Rgc2 maintain Fps1 in an open-channel state by binding to its C-terminal cytoplasmic domain. Phosphorylation of Rgc1 and Rgc2 by Hog1 induces their eviction from Fps1 and consequent channel closure. In the absence of Fps1 channel function, cells experience chronic cell wall stress, which may be exploited for anti-fungal drug development. We show here that Rgc1 and Rgc2 form homo-dimers and heterodimers with each other and that dimer formation of Rgc2 is mediated by its N-terminal domain. Mutations that prevent Rgc2 dimerization block its ability to open Fps1. Therefore, the Rgc - Rgc dimer interface might be an attractive drug target. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 05/2015; DOI:10.1128/EC.00073-15
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    ABSTRACT: The yeast exocyst is a multiprotein complex, comprised of eight subunits (Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70 and Exo84), which orchestrates trafficking of exocytic vesicles to specific docking sites on the plasma membrane during polarized secretion. To study SEC6 function in C. albicans, we generated a conditional mutant strain in which SEC6 was placed under the control of a tetracycline-regulated promoter. In the repressed state, the tetR-SEC6 mutant strain (denoted as tSEC6) was viable for up to 27 h; thus, all phenotypic analyses were performed at 24 h or earlier. Strain tSEC6 under repressing conditions had readily apparent defects in cytokinesis and endocytosis, and accumulated both post-Golgi secretory vesicles and structures suggestive of late endosomes. Strain tSEC6 was markedly defective in secretion of aspartyl proteases and lipases, as well as filamentation under repressing conditions. Lack of SEC6 expression resulted in markedly reduced lateral hyphal branching, which requires the establishment of a new axis of polarized secretion. Aberrant localization of chitin at the septum and increased resistance to zymolyase activity were observed, suggesting that C. albicans Sec6p plays an important role in mediating trafficking and delivery of cell wall components. The tSEC6 mutant was also markedly defective in macrophage killing, indicating a role of SEC6 in C. albicans virulence. Taken together, these studies indicate that the late secretory protein Sec6 is required for polarized secretion, hyphal morphogenesis, and for pathogenesis of C. albicans. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 05/2015; DOI:10.1128/EC.00028-15
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    ABSTRACT: NDR (nuclear Dbf2-related) kinases are essential components for polarized morphogenesis, cytokinesis, cell proliferation, and apoptosis. The NDR kinase Cbk1 is required for the hyphal growth of Candida albicans; however, the molecular functions of Cbk1 in hyphal morphogenesis are largely unknown. Here we report that Ckb1 down-regulates the transcriptional repressor Nrg1 through the mRNA-binding protein Ssd1, which has nine Cbk1 phosphorylation consensus motifs. We found that deletion of SSD1 partially suppressed the defective hyphal growth of the C. albicans cbk1Δ/Δ mutant, and that Ssd1 physically interacts with Cbk1. Cbk1 was required for Ssd1 localization to polarized growth sites. The phospho-mimetic SSD1 allele (ssd1-9E) allowed the cbk1Δ/Δ mutant to form short hyphae, and the phospho-deficient SSD1 allele (ssd1-9A) resulted in shorter hyphae compared to the wild type SSD1 allele, indicating that Ssd1 phosphorylation by Cbk1 is important for hyphal morphogenesis. Furthermore, we show that the transcriptional repressor Nrg1 does not disappear during hyphal initiation in the cbk1Δ/Δ mutant but is completely absent in the cbk1Δ/Δ ssd1Δ/Δ double mutant. Deletion of SSD1 also increased Als3 expression and internalization of the cbk1Δ/Δ mutant in the human embryonic kidney cell line HEK293T. Collectively, our results suggest that one of the Cbk1 functions in the hyphal morphogenesis of C. albicans is to down-regulate Nrg1 through Ssd1. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 05/2015; DOI:10.1128/EC.00016-15
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    ABSTRACT: Phosphotransacetylase (Pta), a key enzyme in bacterial metabolism, catalyzes the reversible transfer of an acetyl group from acetyl phosphate to CoA to produce acetyl-CoA and Pi. Two classes of Pta have been identified based on the absence (Pta(I)) or presence (Pta(II)) of an N-terminal regulatory domain. Pta(I) has been fairly well studied in bacteria and one genus of archaea; however, only the Escherichia coli and Salmonella enterica Pta(II) enzymes have been biochemically characterized, and both are allosterically regulated. Here we describe the first biochemical and kinetic characterization of a eukaryotic Pta from the oomycete Phytophthora ramorum. The two Ptas from P. ramorum, designated as PrPta(II)1 and PrPta(II)2, both belong to class II. PrPta(II)1 displayed positive cooperativity for both acetyl phosphate and CoA and is allosterically regulated. We compared the effect of different metabolites on PrPta(II)1 and the S. enterica Pta(II) and found that although the N-terminal regulatory domains share only 19% identity, both enzymes are inhibited by ATP, NADP, NADH, PEP, and pyruvate in the acetyl-CoA/Pi-forming direction but are differentially regulated by AMP. Phylogenetic analysis of bacterial, archaeal, and eukaryotic sequences identified four subtypes of Pta(II) based on the presence or absence of the P-loop and DRTGG subdomains within the N-terminal regulatory domain. Although the E. coli, S. enterica, and P. ramorum enzymes all belong to the IIa subclass, our kinetic analysis has indicated that enzymes within a subclass can still display differences in their allosteric regulation. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 05/2015; DOI:10.1128/EC.00007-15
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    ABSTRACT: Chitin is an essential component of the fungal cell wall providing rigidity and stability. Its degradation is mediated by chitinases and supposedly ensures dynamic plasticity of the cell wall during growth and morphogenesis. Hence, chitinases should be particularly important for fungi with dramatic morphological changes such as Ustilago maydis. This smut fungus switches from yeast to filamentous growth for plant infection, proliferates as a mycelium in planta and forms teliospores for spreading. Here, we investigate the contribution of its four chitinolytic enzymes to the different morphological changes during the complete life cycle in a comprehensive study of deletion strains combined with biochemical and cell biological approaches. Interestingly, two chitinases act redundantly in cell separation during yeast growth. They mediate the degradation of remnant chitin in the fragmentation zone between mother and daughter cell. By contrast, even the complete lack of chitinolytic activity does not affect formation of the infectious filament, infection, biotrophic growth or teliospore germination. Thus, unexpectedly we can exclude a major role for chitinolytic enzymes in morphogenesis or pathogenicity of U. maydis. Nevertheless, redundant activity of even two chitinases is essential for cell separation during saprophytic growth possibly to improve nutrient access or spreading of yeast cells by wind or rain. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 05/2015; DOI:10.1128/EC.00022-15
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    ABSTRACT: Important for the lifestyle and survival of every organism is the ability to respond to changing environmental conditions. The necrotrophic plant pathogen Botrytis cinerea triggers an oxidative burst in the course of plant infection and therefore needs efficient signal transduction to cope with this stress. The factors involved in this process and their precise roles are still not well known. Here we show that the transcription factor Bap1 and the response regulator (RR) BcSkn7 are two key players in the oxidative stress response (OSR) of B. cinerea; both have major influence on the regulation of classical OSR genes. A Yeast-one-hybrid (Y1H) approach proved direct binding to the promotors of gsh1 and grx1 by Bap1 and of glr1 by BcSkn7. While the function of Bap1 is restricted to the regulation of oxidative stress, analyses of Δbcskn7 mutants revealed functions beyond OSR. Involvement of BcSkn7 in development and virulence could be demonstrated, indicated by reduced vegetative growth, impaired formation of reproductive structures, and reduced infection cushion-mediated penetration of the host by the mutants. Furthermore, Δbcskn7 mutants were highly sensitive to oxidative, osmotic and cell wall stress. Analyses of ΔΔbap1bcskn7 double mutants indicated that loss of Skn7 uncovers an underlying phenotype of Bap1. In contrast to yeast, the ortholog of the glutathione peroxidase Gpx3p is not required for nuclear translocation of Bap1. The presented results contribute to the understanding of the OSR in B. cinerea and prove that it differs substantially from yeast, demonstrating the complexity and versatility of components involved in signaling pathways. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Eukaryotic Cell 05/2015; DOI:10.1128/EC.00043-15