The calmodulin-dependent protein phosphatase catalytic subunit (calcineurin A) is an essential gene in Aspergillus nidulans.

Rasmussen, Colin D.; Garen, Craig R.; Brining, Sheryl K.; Kincaid, Randall L.; Means, Raylene L.; Means, Anthony R.

doi:10.1002/j.1460-2075.1994.tb06703.x

Cited by 67 publications

(72 citation statements)

References 11 publications

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“…In yeast, for example, 11 more targets for CaM other than calcineurin were identified (851). The calmodulin/calcineurin signaling pathway is required for appropriate stress responses, mitosis, growth (852)(853)(854), and other pathways, like toxin production (855). In T. reesei, calmodulin was shown to be essential for secretion of xylanases (839).…”

Section: Genomes Of T Reesei T Virens and T Atroviride Respectimentioning

confidence: 99%

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

Schmoll

Dattenböck

Carreras-Villaseñor

et al. 2016

Microbiol Mol Biol Rev

165

195

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SUMMARYThe genusTrichodermacontains fungi with high relevance for humans, with applications in enzyme production for plant cell wall degradation and use in biocontrol. Here, we provide a broad, comprehensive overview of the genomic content of these species for “hot topic” research aspects, including CAZymes, transport, transcription factors, and development, along with a detailed analysis and annotation of less-studied topics, such as signal transduction, genome integrity, chromatin, photobiology, or lipid, sulfur, and nitrogen metabolism inT. reesei,T. atroviride, andT. virens, and we open up new perspectives to those topics discussed previously. In total, we covered more than 2,000 of the predicted 9,000 to 11,000 genes of eachTrichodermaspecies discussed, which is >20% of the respective gene content. Additionally, we considered available transcriptome data for the annotated genes. Highlights of our analyses include overall carbohydrate cleavage preferences due to the different genomic contents and regulation of the respective genes. We found light regulation of many sulfur metabolic genes. Additionally, a new Golgi 1,2-mannosidase likely involved inN-linked glycosylation was detected, as were indications for the ability ofTrichodermaspp. to generate hybrid galactose-containingN-linked glycans. The genomic inventory of effector proteins revealed numerous compounds unique toTrichoderma, and these warrant further investigation. We found interesting expansions in theTrichodermagenus in several signaling pathways, such as G-protein-coupled receptors, RAS GTPases, and casein kinases. A particularly interesting feature absolutely unique toT. atrovirideis the duplication of the alternative sulfur amino acid synthesis pathway.

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Section: Genomes Of T Reesei T Virens and T Atroviride Respectimentioning

confidence: 99%

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

Schmoll

Dattenböck

Carreras-Villaseñor

et al. 2016

Microbiol Mol Biol Rev

165

195

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“…CaM-dependent protein kinase II has also been found to be involved in the onset and progression of mitosis (35,36). Finally, the involvement of calcineurin in the onset of DNA replication has been described recently (52).…”

Section: Calmodulin (Cam) Is a Ubiquitous Ca 2ϩmentioning

confidence: 99%

Phosphorylation of Rat Liver Heterogeneous Nuclear Ribonucleoproteins A2 And C Can be Modulated by Calmodulin

Bosser

Faura

Serratosa

et al. 1995

Molecular and Cellular Biology

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). By immunoblotting, peptide mapping, and endogenous phosphorylation experiments, the 36-and 40-to 42-kDa proteins have been identified as the A2 and C proteins, respectively, of the heterogeneous nuclear ribonucleoprotein particles. To better understand the mechanism by which calmodulin inhibits the phosphorylation of these proteins, they were purified by using single-stranded DNA chromatography, and the effect of calmodulin on their phosphorylation by casein kinase 2 was analyzed. Results revealed that whereas calmodulin inhibited the phosphorylation of purified A2 and C proteins in a Ca 2؉ -dependent manner, it did not affect the casein kinase 2 phosphorylation of a different protein substrate, i.e., ␤-casein. These results indicate that the effect of calmodulin was not on casein kinase 2 activity but on specific protein substrates. The finding that the A2 and C proteins can bind to a calmodulin-Sepharose column in a Ca 2؉ -dependent manner suggests that this association could prevent the phosphorylation of the proteins by casein kinase 2. Immunoelectron microscopy studies have revealed that such interactions could also occur in vivo, since calmodulin and A2 and C proteins colocalize on the ribonucleoprotein particles in rat liver cell nuclei. Calmodulin (CaM) is a ubiquitous Ca 2ϩ-binding protein which has been highly conserved during evolution. The binding of Ca 2ϩ to CaM induces a conformational change which permits the interaction of CaM with specific target proteins, i.e., CaM-binding proteins. During the last few years, compelling evidence indicating that CaM is present in the cell nucleus (4) and that it has a role in several nuclear functions, such as gene transcription (21), DNA replication, DNA repair, and mitosis (see references 3, 4, and 36 for reviews), has accumulated.One of the ways to understand the molecular mechanisms by which CaM regulates these nuclear functions has been the identification of its nuclear protein targets. At least three groups of CaM-binding proteins have been found in the nuclei of different cell types: (i) proteins related to the actin motility systems, e.g., ␣-spectrin, myosin light-chain kinase, and caldesmon (6, 51, 57); (ii) transcription factors belonging to the basic helix-loop-helix structural group, e.g., human SEF-1, mouse E2A, and Max (21); and (iii) proteins involved in the phosphorylation or dephosphorylation of proteins, e.g., CaM-dependent protein kinase II and the CaM-dependent protein phosphatase calcineurin (11,51,54). The role of the specific complexes of CaM with these CaM-binding proteins in the nuclear functions still remains obscure, although some possible pathways have recently emerged. It has recently been reported that the addition of antiactin antibodies blocks the transport of macromolecules into purified nuclei in in vitro experiments, suggesting that the nuclear actin-myosin contractile system can play a role in nucleocytoplasmic transport (55). The transcription factors which are able to bind CaM and belong to the basic helix-loop-helix grou...

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“…To confirm that pinA is essential in A. nidulans we disrupted the gene in a heterokaryon in a manner similar to that described for cmkA, cmkB, CaM, and cnaA (27,(33)(34)(35). As diagramed in Fig.…”

Section: Pina Is Essential In Aspergillus Nidulans-to Address Thementioning

confidence: 99%

PINA Is Essential for Growth and Positively Influences NIMA Function in Aspergillus nidulans

Joseph

Daigle²,

Means

2004

Journal of Biological Chemistry

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The phospho-Ser/Thr-directed prolyl-isomerase Pin1 was originally identified in vertebrate systems as a negative regulator of NIMA, a Ser/Thr protein kinase that regulates the G 2 /M transition in Aspergillus nidulans. Here we explore the physiological roles of the Pin1 orthologue, PINA, in A. nidulans and evaluate the relevance of the interaction of PINA with NIMA in this fungus. We find pinA to be an essential gene in A. nidulans. In addition, when PINA levels are reduced 50-fold the cells grow at a reduced rate. Upon germination under conditions that repress PINA expression, the cells are delayed in the interphase activation of NIMX cdc2 , whereas they traverse the other phases of the cell cycle at a similar rate to controls. These results indicate that a marked reduction of PINA results in a lengthening of G 1 . Additionally, PINA repression increases the rate at which the cells enter mitosis following release from a hydroxyurea arrest without altering the sensitivity of the fungus to agents that activate the replication or DNA damage checkpoints. In contrast to predictions based on Pin1, the physical interaction between PINA and NIMA is primarily dependent upon the prolylisomerase domain of PINA and the C-terminal 303 amino acids of NIMA. Finally, reduction of PINA levels exacerbates the nimA5 temperature-sensitive mutant, whereas overexpression of PINA decreases the severity of this mutation, results that are consistent with a positive genetic interaction between PINA and NIMA. Thus, although PINA is essential and positively regulates NIMA function, A. nidulans is most sensitive to a reduction in PINA concentration in G 1 rather than in G 2 /M.

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The calmodulin-dependent protein phosphatase catalytic subunit (calcineurin A) is an essential gene in Aspergillus nidulans.

Cited by 67 publications

References 11 publications

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

Phosphorylation of Rat Liver Heterogeneous Nuclear Ribonucleoproteins A2 And C Can be Modulated by Calmodulin

PINA Is Essential for Growth and Positively Influences NIMA Function in Aspergillus nidulans

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