A homologue of the human STRIPAK complex controls sexual development in fungi

Bloemendal, Sandra; Bernhards, Yasmine; Bartho, Kathrin; Dettmann, Anne; Voigt, Oliver; Teichert, Ines; Seiler, Stephan; Wolters, Dirk; Pöggeler, Stefanie; Kück, Ulrich

doi:10.1111/j.1365-2958.2012.08024.x

Cited by 100 publications

(238 citation statements)

References 57 publications

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“…For the generation of transgenic plasmids, homologous recombination in S. cerevisiae PJ69-4a and standard cloning procedures were used (James et al 1996;Sambrook and Russell 2001;Colot et al 2006;Bloemendal et al 2012). To allow homologous recombination of nox knockout constructs in S. macrospora Δku70, the flanking regions of the corresponding nox genes together with the hph resistance cassette were inserted into pRS426 (Christianson et al 1992).…”

Section: Genome Sequencing Of Developmental Mutant Pro32mentioning

confidence: 99%

“…Cleaning of raw data, mapping to the S. macrospora reference genome, and analysis of sequence variants were performed as previously described Generation of Dnox1, Dnox2, and Dnor1 deletion strains Transformation of S. macrospora was performed as described previously with an enzyme mix of 1 g VinoTaste Pro (Novozymes, Blagsvaerd, Denmark), 0.3 g Caylase (Cayla, Toulouse, France), and 27 U Chitinase (ASA Spezialenzyme, Wolfenbüttel, Germany) (Walz and Kück 1995;Engh et al 2007). For the generation of transgenic plasmids, homologous recombination in S. cerevisiae PJ69-4a and standard cloning procedures were used (James et al 1996;Sambrook and Russell 2001;Colot et al 2006;Bloemendal et al 2012). To allow homologous recombination of nox knockout constructs in S. macrospora Δku70, the flanking regions of the corresponding nox genes together with the hph resistance cassette were inserted into pRS426 (Christianson et al 1992 Plasmids for complementation of nox deletion strains were generated as follows: the nox ORFs and 1000 kb up-and downstream regions were amplified via PCR [nox1: 05007-5fw/05007-3rv (3889 bp); nox2: 08742-5fw/08742-3rv (3709 bp); nor1: 02124-5fw/02124-3rv (3842 bp)].…”

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New Insights Into the Roles of NADPH Oxidases in Sexual Development and Ascospore Germination in Sordaria macrospora

et al. 2014

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NADPH oxidase (NOX)-derived reactive oxygen species (ROS) act as signaling determinants that induce different cellular processes. To characterize NOX function during fungal development, we utilized the genetically tractable ascomycete Sordaria macrospora. Genome sequencing of a sterile mutant led us to identify the NADPH oxidase encoding nox1 as a gene required for fruiting body formation, regular hyphal growth, and hyphal fusion. These phenotypes are shared by Δnor1, lacking the NOX regulator NOR1. Further phenotypic analyses revealed a high correlation between increased ROS production and hyphal fusion deficiencies in Δnox1 and other sterile mutants. A genome-wide transcriptional profiling analysis of mycelia and isolated protoperithecia from wild type and Δnox1 revealed that nox1 inactivation affects the expression of genes related to cytoskeleton remodeling, hyphal fusion, metabolism, and mitochondrial respiration. Genetic analysis of Δnox2, lacking the NADPH oxidase 2 gene, Δnor1, and transcription factor deletion mutant Δste12, revealed a strict melanin-dependent ascospore germination defect, indicating a common genetic pathway for these three genes. We report that gsa3, encoding a G-protein a-subunit, and sac1, encoding cAMP-generating adenylate cyclase, act in a separate pathway during the germination process. The finding that cAMP inhibits ascospore germination in a melanin-dependent manner supports a model in which cAMP inhibits NOX2 activity, thus suggesting a link between both pathways. Our results expand the current knowledge on the role of NOX enzymes in fungal development and provide a frame to define upstream and downstream components of the NOX signaling pathways in fungi. D URING sexual reproduction, filamentous fungi generate complex fruiting bodies that contain and protect meiosporangia. We used the ascomycetous model fungus Sordaria macrospora to identify genes directly involved in fruiting body development (Kück et al. 2009;Engh et al. 2010;Kück et al. 2009). Due to its homothallic life style, S. macrospora is able to complete the sexual life cycle without the mating of strains with opposite sex, and therefore, fruiting body-deficient mutants can be recognized directly without the need for crossing experiments. In earlier work, we generated sterile mutants showing a developmental block after formation of young fruiting bodies (protoperithecia), but being unable to generate mature perithecia, and referred to these mutants as pro. Recently, we have applied next-generation genome re-sequencing to identify the genes affected in some of these mutants . Based on this approach, we now have characterized mutant pro32 and show that it carries a mutation in the nox1 gene encoding NAPDH oxidase 1 (NOX1).NADPH oxidase (NOX) enzymes are transmembrane proteins that are highly conserved among eukaryotes and produce reactive oxygen species (ROS) through the oxidation of NADPH (Lambeth 2004;Kawahara and Lambeth 2007). ROS have long been recognized as damaging agents due to uncontrolled oxidizing re...

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Section: Genome Sequencing Of Developmental Mutant Pro32mentioning

confidence: 99%

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confidence: 99%

New Insights Into the Roles of NADPH Oxidases in Sexual Development and Ascospore Germination in Sordaria macrospora

et al. 2014

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“…Human Striatin 3 and its Sordaria macrospora ortholog PRO11 have been reported to contain an N-terminal coiled-coil region, and both proteins are critical components in the organization of their respective STRIPAK complexes (3,18). Like human striatins, yeast Far8 was also predicted to contain an N-terminal coiled-coil domain (22,25).…”

Section: Discussionmentioning

confidence: 99%

“…In Neurospora crassa, orthologs of STRIPAK complex components are required for hyphal fusion (16,17). In the ascomycete Sordaria macrospora, the STRIPAK complex is required for sexual development and vegetative hyphal fusion (18,19). In the fission yeast Schizosaccharomyces pombe, components of the STRIPAK complex localize to the mitotic spindle pole body in early mitosis and are required for the establishment of asymmetry of the septation initiation network, a conserved signaling pathway that is required for cytokinesis and mitotic transitions (9,20).…”

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Tiered Assembly of the Yeast Far3-7-8-9-10-11 Complex at the Endoplasmic Reticulum

Pracheil

Liu

2013

Journal of Biological Chemistry

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Background: The Far3-7-8-9-10-11 complex, part of the yeast striatin-interacting phosphatase and kinase (STRIPAK) complex, mediates target of rapamycin complex 2 (TORC2) signaling. Results: The Far3-7-8-9-10-11 complex follows tiered assembly at the endoplasmic reticulum (ER). Conclusion: ER localization of Far9 is required for optimal function in TORC2 signaling. Significance: Our study provides insights into the organization of the yeast STRIPAK complex.

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“…Cell debris was sedimented via centrifugation, and the supernatant was applied to TAP according to the work of Bayram et al (37) as described elsewhere (38).…”

Section: Methodsmentioning

confidence: 99%

Identification of a Chloroplast Ribonucleoprotein Complex Containing Trans-splicing Factors, Intron RNA, and Novel Components

Jacobs

Marx

Kock

et al. 2013

Molecular & Cellular Proteomics

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Maturation of chloroplast psaA pre-mRNA from the green alga Chlamydomonas reinhardtii requires the trans-splicing of two split group II introns. Several nuclear-encoded trans-splicing factors are required for the correct processing of psaA mRNA. Among these is the recently identified Raa4 protein, which is involved in splicing of the tripartite intron 1 of the psaA precursor mRNA. Part of this tripartite group II intron is the chloroplast encoded tscA RNA, which is specifically bound by Raa4. Using Raa4 as bait in a combined tandem affinity purification and mass spectrometry approach, we identified core components of a multisubunit ribonucleoprotein complex, including three previously identified trans-splicing factors (Raa1, Raa3, and Rat2). We further detected tscA RNA in the purified protein complex, which seems to be specific for splicing of the tripartite group II intron. Intron-containing genes from prokaryotic or organellar genomes carry either group I or group II introns, each of which has distinct features. The splicing mechanism of group II introns and the secondary structures of their presumed active sites were used as early arguments for the hypothesis that this class of introns represents the ancestors of eukaryotic spliceosomal introns (1, 2). It was further assumed that group II introns invaded the eukaryotic nucleus and subsequently proliferated at various genomic sites, leading to the degeneration of the catalytic intron structure into small nuclear RNAs (snRNAs).1 This assumption was supported by the observation of naturally occurring variants of group II introns that are split into two or more pieces (3), reminiscent of eukaryotic spliceosomal RNA (1). Group II intron RNAs are characterized by six conserved domains, and tertiary interactions among these domains generate the compact native and catalytic complex. Some of these group II intron domains have been shown to act in trans on the splicing of other introns that lack the corresponding domain (4). In vivo, various RNA-binding proteins promote the formation of catalytically active intron RNA. In contrast to the nuclear spliceosome, which acts generally on a broad range of nuclear-encoded pre-mRNAs, proteins involved in organellar intron splicing seem to more efficiently stabilize the active three-dimensional RNA structure in vivo. Several splicing factors in higher plants, such as the chloroplast RNA-splicing and ribosome maturation (CRM) domain protein CRS1, as well as the pentatricopeptide repeat proteins OTP51 and PPR4, have been reported to be involved in the splicing of single transcripts (5, 6). Nonetheless, there are splicing factors that carry out functions on a broad range of transcripts, including CRS2 and its associated proteins CAF1 and CAF2, and WTF1, a splicing factor containing a plant organelle RNA-recognition domain (5, 6). Sedimentation and co-fractionation experiments in, for example, maize have demonstrated that these proteins are part of large multiprotein and ribonucleoprotein complexes with their cognate RNAs (5, 7). I...

show abstract

A homologue of the human STRIPAK complex controls sexual development in fungi

Cited by 100 publications

References 57 publications

New Insights Into the Roles of NADPH Oxidases in Sexual Development and Ascospore Germination in Sordaria macrospora

New Insights Into the Roles of NADPH Oxidases in Sexual Development and Ascospore Germination in Sordaria macrospora

Tiered Assembly of the Yeast Far3-7-8-9-10-11 Complex at the Endoplasmic Reticulum

Identification of a Chloroplast Ribonucleoprotein Complex Containing Trans-splicing Factors, Intron RNA, and Novel Components

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