Peptide utilization by nitrogen-starved Neurospora crassa

Wolfinbarger, Lloyd; Snyder, F. W.; Castellano, José María

doi:10.1128/jb.153.3.1567-1569.1983

Cited by 4 publications

(3 citation statements)

References 11 publications

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“…In contrast to the results of the present study, Wolfinbarger, Snyder & Castellano (1983), working with N. crassa found a systematic increase in proteinase production in response to increasing polymerization in a heterogeneous peptide series ranging from amino acids to peptides of an average 5 amino acid residues. Further increasing the size of the peptides, to a mean value of 30 amino acid residues, caused an exponential increase in proteinase production.…”

Section: Discussioncontrasting

confidence: 99%

“…The much greater proteinase activity in culture grown with ammonium, relative to that in cultures exposed to alanine or its oligopeptides is noteworthy in view of earlier reports that mineral N was particularly effective at repressing proteinase production in Neurospora (Wolfinbarger et al, 1983) and A. nidulans (Cohen, 1973). However the results are comparable with those of Kalisz et al (1987) who showed that the production of proteinases by A. bisporus, C. cinereus and V. volvacea was not repressed by ammonium.…”

Section: Discussionmentioning

confidence: 70%

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Proteinase activity in mycorrhizal fungi

Leake¹,

Read²

1990

New Phytologist

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SUMMARYThe ericoid mycorrhizal endophyte, Hymenoscyphus ericae (Read) Korf & Kernan, was grown in liquid media containing either ammonium, the amino acid alanine, peptide (di-, tri-, tetra-or hexa-alanine), or bovine serum albumin (BSA) as sole nitrogen (N) source. The effects of the various N sources upon production of extracellular acid proteinase, its specific activity and growth of the fungus were determined.While extracellular acid proteinase was induced in the presence of each N source, enzyme production was considerably enhanced in the culture grown with BSA. Total enzyme activity in the culture solutions declined in the order BSA ^ ammonium > peptides and alanine. Enzyme activity per mg dry weight of mycelium was greatest in the presence of BSA.Similar yields of fungal mycelium and rates of growth were observed regardless of N source. The results are discussed in relation to quantitative aspects of the N status of heathland soils.

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Section: Discussioncontrasting

confidence: 99%

Section: Discussionmentioning

confidence: 70%

Proteinase activity in mycorrhizal fungi

Leake¹,

Read²

1990

New Phytologist

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“…It is not clear in A. nidulans how large a peptide can be transported without prior extracellular degradation. In Neurospora crassa (Wolfinbarger et al, 1983) and in yeast (Marder et al, 1977) pentapeptides appear to be the upper limit. The principal extracellular proteinase, proteinase 11, degrades a wide range of proteins (Ansari & Stevens, 19836).…”

Section: Characterization Of' Proteinases and Peptidusementioning

confidence: 95%

Regulation of proteinase activity in Aspergillus nidulans

Stevens

1985

Biochemical Society Transactions

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1976) which is a defective in killer toxin secretion and in secretion of mature a-factor (T. Achstetter & D. H. Wolf, unpublished work). With the aid of the two model substrates, Cbz-Tyr-Lys and Cbz-Tyr-Lys-Arg, we also found carboxypeptidase activity in the membrane fraction, which is able to remove the two amino acids lysine and arginine and may thus be involved in further processing of the a-factor molecule. The enzyme was named carboxypeptidase ysca (T. Achstetter & D. H. Wolf, unpublished work). Another proteolytic process is involved in the biogenesis of the vacuole, the lysosome-like cell compartment of yeast. Carboxypeptidase yscY (Hasilik & Tanner, 1978) and the two endoproteinases yscA and yscB (Mechler et al., 1982) were found to be synthesized as precursor molecules of M , 67000, 52000 and 42000 respectively, which undergo proteolytic processing to yield their mature forms of M , 61 000, 42000 and 33000 respectively. The function of the putative processing proteinase most likely resides in the activation of the enzymes. Proteinase yscB had been proposed to be the processing enzyme for the carboxypeptidase yscY precursor (Hasilik & Tanner, 1978). However, studies on mutants lacking proteinase yscB ruled out this possibility (Wolf & Ehmann, 1979; Hemmings et al., 1981). No new candidate proteinase for the processing process has yet been found. Table 2 summarizes our present knowledge on the yeast proteinases and their functions. Large gaps concerning their function still exist. It is not hard to guess that the number of proteinases presented in Table 2 will most likely increase when more studies are done.

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Phase I study of beta-alanyl-melphalan as a potent anticancer drug

Tsay

Wolfinbarger

1987

Cancer Chemother. Pharmacol.

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The dipeptide beta-alanyl-melphalan was synthesized and tested for its potential anticancer activity. It is shown to possess considerable toxicity toward Ehrlich ascites tumor cells and 3T3 mouse embryo cells in in vitro toxicity assays and is a potent anticancer agent when used in vivo in traditional phase I chemotherapy assays. The potential role for small peptide transport mechanisms in transportation of anticancer agents is discussed.

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Peptide utilization by nitrogen-starved Neurospora crassa

Cited by 4 publications

References 11 publications

Proteinase activity in mycorrhizal fungi

Proteinase activity in mycorrhizal fungi

Regulation of proteinase activity in Aspergillus nidulans

Phase I study of beta-alanyl-melphalan as a potent anticancer drug

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