A novel stimulator of protein phosphorylation in Neurospora crassa

Ulloa, Rita M.; Glikin, Gerardo C.; Téllez-Iñón, Marı́a T.; Torres, Héctor N.; Judewicz, Norberto D.

doi:10.1007/bf00230146

Cited by 6 publications

(7 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…They found that purified PK-III was inhibited by fenpiclonil and fludioxonil (Pillonel and Meyer, 1997). Although the concentration of phenylpyrroles required for PK-III inhibition was found similar to that of rat PKC-inhibition, N. crassa PK-III does not seem to be neither a Ca 2+ /calmodulin nor a cAMP regulated protein kinase (Judewicz et al, 1981; Ulloa et al, 1987). To some extend the inhibition of PK-III correlated with growth inhibition by fenpiclonil, but less by fludioxonil, raising the question if phenylpyrroles, especially fenpiclonil, directly inhibit PK-III activity.…”

Section: Effect Of Phenylpyrroles On Target Fungi – Mode Of Actionmentioning

confidence: 85%

Phenylpyrroles: 30 Years, Two Molecules and (Nearly) No Resistance

Kilani¹,

Fillinger²

2016

Front. Microbiol.

106

View full text Add to dashboard Cite

Phenylpyrroles are chemical analogs of the natural antifungal compound pyrrolnitrin. Fenpiclonil, but mainly fludioxonil are registered against multiple fungal crop diseases since over 25 years for seed or foliar treatment. They have severe physiological impacts on the pathogen, including membrane hyperpolarization, changes in carbon metabolism and the accumulation of metabolites leading to hyphal swelling and burst. The selection and characterization of mutants resistant to phenylpyrroles have revealed that these fungicides activate the fungal osmotic signal transduction pathway through their perception by a typical fungal hybrid histidine kinase (HHK). The HHK is prone to point mutations that confer fungicide resistance and affect its sensor domain, composed of tandem repeats of HAMP motifs. Fludioxonil resistant mutants have been selected in many fungal species under laboratory conditions. Generally they present severe impacts on fitness parameters. Since only few cases of field resistance specific to phenylpyrroles have been reported one may suspect that the fitness penalty of phenylpyrrole resistance is the reason for the lack of field resistance.

show abstract

Section: Effect Of Phenylpyrroles On Target Fungi – Mode Of Actionmentioning

confidence: 85%

Phenylpyrroles: 30 Years, Two Molecules and (Nearly) No Resistance

Kilani¹,

Fillinger²

2016

Front. Microbiol.

106

View full text Add to dashboard Cite

show abstract

“…When acid substrates such as phosvitin or casein were used as acceptors, the reaction was stopped with 10% TCA according to Ulloa et al (1987). The Ko.5 for Ca2+ was determined in the presence of EGTA-Ca2+ buffers according to Bartfai (1979).…”

Section: Protein Kinase Activity Assaysmentioning

confidence: 99%

Changes in Calcium-Dependent Protein Kinase Activity during in Vitro Tuberization in Potato

et al. 1996

View full text Add to dashboard Cite

show abstract

“…A wild type Neurospora crassa strain (St. Lawrence 74) was grown in Vogel's minimal medium supplemented with 2% (w/v) sucrose and 2.5tzg/ml dbiotin as described [4]. Cultures were shaken (100 oscillations/min) at 30°C in 1000 ml Erlenmeyer flasks containing 200 ml medium in a rotatory air incubator.…”

Section: Culturesmentioning

confidence: 99%

“…A second one is dependent on Ca 2+ and calmodulin [3]. A third type of mechanism involves a protein kinase, specific for phosvitin, which is activated by an endogenous thermostable peptide [4]. Recently, a fourth type of regulatory mechanism was described involving a Ca 2+phospholipid dependent protein kinase C [5].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Ca2+ calmodulin-dependent protein kinase activity in the ascomycetes Neurospora crassa

et al. 1991

View full text Add to dashboard Cite

DEAE-cellulose column chromatography of Neurospora crassa soluble mycelial extracts leads to the resolution of three major protein kinase activity peaks designated PKI, PKII, and PKIII. PKII activity is stimulated by Ca2+ and Neurospora or brain calmodulin. Maximal stimulation was observed at 2 microM-free Ca2+ and 1 microgram/ml of the modulator. The stimulatory effect of the Ca(2+)-calmodulin complex was blocked by EGTA and by some calmodulin antagonists such as phenothiazine drugs or compound 48/80. PKII phosphorylates different proteins, among which histone II-A at a low concentration and CDPKS, the synthetic peptide specific for Ca(2+-)-calmodulin dependent protein kinase, are the best substrates. Some phosphorylation can be detected in the absence of any exogenous acceptor. PKII activity assayed in the presence of histone II-A or in the absence of exogenous phosphate acceptor (autophosphorylation) co-elute in a DEAE-cellulose column at 0.28 NaCl. As result of the autophosphorylation reaction of the purified enzyme a main phosphorylated component of 70 kDa was resolved by SDS-polyacrylamide gel electrophoresis. It is possible that this component is an active part of this enzyme.

show abstract

A novel stimulator of protein phosphorylation in Neurospora crassa

Cited by 6 publications

References 8 publications

Phenylpyrroles: 30 Years, Two Molecules and (Nearly) No Resistance

Phenylpyrroles: 30 Years, Two Molecules and (Nearly) No Resistance

Changes in Calcium-Dependent Protein Kinase Activity during in Vitro Tuberization in Potato

Ca2+ calmodulin-dependent protein kinase activity in the ascomycetes Neurospora crassa

Contact Info

Product

Resources

About