Derepression of tyrosinase synthesis in Neurospora by amino acid analogs

Horowitz, N. H.; Fling, Marguerite; Feldman, Helen Macleod; Pall, Martin L.; Froehner, Stanley C.

doi:10.1016/0012-1606(70)90066-7

Cited by 46 publications

(24 citation statements)

References 15 publications

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“…Horowitz et al (16) showed that de novo synthesis of tyrosinase can be induced by suspension of stationary-phase Neurospora cultures in phosphate buffer or, paradoxically, by addition of amino acid analogs (17) of Neiurospora circadian rhythmicity, we found that pulses of CHX reset the circadian clock and that the amount of resetting is concentration dependent (28). To further investigate this phenomenon, we examined protein synthesis patterns in the presence of various concentrations of CHX.…”

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confidence: 85%

Cycloheximide and heat shock induce new polypeptide synthesis in Neurospora crassa.

Perlman¹,

Feldman²

1982

Mol. Cell. Biol.

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Treatment of Neurospora crassa with 0.1 microgram of cycloheximide per ml, a concentration which inhibited protein synthesis by about 70%, resulted in the greatly enhanced synthesis of at least three polypeptide bands with estimated molecular weights of 88,000, 30,000, and 28,000. A temperature shift from 25 to 37 degrees C resulted in the appearance of a single new polypeptide band of 70,000 daltons, the same size as the major heat shock-induced proteins observed in species of Drosophila and Dictyostelium. Synthesis of the cycloheximide-stimulated polypeptide bands was on cytoplasmic ribosomes rather than on mitochondrial ribosomes, as incorporation of isotope into the polypeptide bands was inhibited by 1.0 microgram of cycloheximide per ml but not by 1 mg of chloramphenicol per ml. In a mutant with cycloheximide-resistant ribosomes, 0.1 microgram of cycloheximide per ml failed to alter the pattern of protein synthesis from that of the controls. It is suggested that the new synthesis of the polypeptide bands reflects specific mechanisms of adaptation to different kinds of environmental stress, including inhibition of protein synthesis and temperature increases.

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mentioning

confidence: 85%

Cycloheximide and heat shock induce new polypeptide synthesis in Neurospora crassa.

Perlman¹,

Feldman²

1982

Mol. Cell. Biol.

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“…There are instances, however, in which CHI similarly mimics an animal hormone or growth factor effect. A long-known case in Neurospora in which inhibitors induce by themselves is the paradoxical induction oftyrosinase (10) and laccase (9). Analogous effects on certain plant systems have also been reported (1 1), including a case where a GS activity is increased by CHI (13).…”

Section: Methodsmentioning

confidence: 99%

Involvement of Macromolecule Biosynthesis in Auxin and Fusicoccin Enhancement of β-Glucan Synthase Activity in Pea

Ray

1987

Plant Physiol.

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In pea stem segments whose cuticle has been made permeable by abrading it, actinomycin D (ActD) and 80S ribosomal protein synthesis inhibitors such as cycloheximide (CHI) inhibit enhancement by indole 3-acetic acid (IAA) of the activity of the cell wall biosynthetic enzyme, glucan synthase I (GS). This supersedes earlier, negative results with inhibitors, obtained with segments having an intact cuticle, which prevents adequate inhibitor uptake. Since these inhibitors also block IAAstimulated H' extrusion, which according to earlier results is involved in the GS response, the significance of these inhibitions would be ambiguous without additional evidence. ActD does not inhibit fusicoccin (FC) enhancement of GS activity, which indicates existence of a post-trnscriptional control mechanism for GS, but does not preclude involvement of transcription in the GS response to IAA. Although protein synthesis inhibitors such as CHI do not block FC-stimulated H' extrusion, they do inhibit FC enhancement of GS activity, indicating an involvement of protein synthesis in the GS response to FC, and presumably also to LAA. However, protein synthesis inhibitors (but not ActD) by themselves paradoxically elevate GS activity, less strongly than IAA does but resembling the UIA enhancement in several characteristics. These results suggest that IAA may enhance GS activity at least in part by inhibiting the synthesis or action of a labile repressor of the transcription of, or a labile destabilizer of, mRNA for GS or some polypeptide that enhances GS activity. However, resemblances between the IAA and FC effects on GS suggest that UIA also has a posttanscriptional GS-enhancing action like that of FC. Lipid biosynthesis may be involved in this aspect of the response since both IAA and FC enhancements of GS activity are inhibited by cerulenin.IAA causes a rapid increase in GS2 activity, in pea third internode tissue segments whose GS activity has declined after isolation from the plant (16). This response, which probably contributes to the auxin stimulation of cell wall synthesis (1) extrusion plays a role in this enhancement (18). To study this I used pea stem segments abraded with emergy particle suspension to make their cuticle H+-permeable, so that IAA-and FCstimulated H+ extrusion could be measured (18). With such tissue I obtained effects of protein and RNA synthesis inhibitors on the GS activity response to auxin that differed importantly from the results I had previously obtained with unabraded tissue. This prompted further investigation of apects of metabolism involved in the GS response to auxin and FC, the outcome of which is presented here. MATERIALS AND METHODSEtiolated pea seedlings, Pisum sativum cv Alaska, were grown, and third internode segments 8 mm long were cut from them, as described previously (1), except that unless stated otherwise the third internode was always abraded with emergy powder paste as described (18) and the internode was rinsed by vigorous agitation in two changes oftap water prior to cutting t...

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“…Almost complete ~ibition of the cold-induced increase is achieved with cycloheximide at a concentration of 5 PM, which is sufficient to inhibit protein synthesis in Neurospora by over 90% [8] . The increase is therefore dependent on cytoplasmic protein synthesis Time after Transfer (IO Fig.…”

Section: Resultsmentioning

confidence: 99%

Cold‐induced increase of glycerol kinase in Neurospora crassa

North

1973

FEBS Letters

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Derepression of tyrosinase synthesis in Neurospora by amino acid analogs

Cited by 46 publications

References 15 publications

Cycloheximide and heat shock induce new polypeptide synthesis in Neurospora crassa.

Cycloheximide and heat shock induce new polypeptide synthesis in Neurospora crassa.

Involvement of Macromolecule Biosynthesis in Auxin and Fusicoccin Enhancement of β-Glucan Synthase Activity in Pea

Cold‐induced increase of glycerol kinase in Neurospora crassa

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