Metabolism of elemental sulphur (S°) during fungal spore germination

1993 ◽  
Vol 39 (8) ◽  
pp. 736-741 ◽  
Author(s):  
Trello Beffa

35S-labelled elemental sulphur (S°) at nontoxic levels (3 μM) was incorporated into sulphur amino acids and glutathione by the spores of the fungus Phomopsis viticola. Incorporation studies were performed with 3 μM 35S° during the pregermination period of P. viticola spores. The free sulphur amino acids and protein sulphur amino acids were purified by column and thin-layer chromatography. During the first minutes of the pregermination process of the spores, the S° was essentially metabolized into free cysteine and glutathione. Detectable concentrations of methionine and homocysteine were measured after 1 h of incubation. Azide (2 mM final concentration), an inhibitor of the mitochondrial respiratory chain at the level of cytochrome oxidase, strongly inhibited the incorporation of S°. In contrast, the uncoupler 2,4-dinitrophenol (15 μM final concentration) and sulphate did not affect the incorporation of S°. The metabolism of 35S° into the protein sulphur amino acids cysteine and methionine during the germination of spores of P. viticola and conidia of Neurospora crassa is also discussed. It appears that S° does not necessarily have to be oxidized to sulphate prior to its incorporation into sulphur amino acids, but could be directly reduced to sulphide at the level of the respiratory chain.Key words: elemental sulphur, assimilation, sulphur amino acids, Phomopsis viticola, Neurospora crassa.


1993 ◽  
Vol 39 (8) ◽  
pp. 731-735 ◽  
Author(s):  
Trello Beffa

The fungitoxic effect of increasing concentrations of elemental sulphur (S°) was studied during the pregermination period of spores of Phomopsis viticola and conidia of Neurospora crassa. High concentrations of S° (> 10 μM final concentration) inhibited respiratory activities strongly and decreased the ATP content of spores and conidia. S° at low concentrations (1 and 3 μM final concentration) did not inhibit the respiratory activities or ATP content of spores and conidia. In spores of P. viticola, low concentrations of S° were reduced by the cells with the production of hydrogen sulphide (H2S), principally at the level of the respiratory chain. However, in the presence of a high concentration of S°, the capacity to reduce S° increased, and was then most probably independent of the respiratory activities. Proteic and nonproteic sulphydryl groups important in cellular metabolism were probably responsible for almost all the reduction of S°. In fact, the addition of increasing concentrations of S° to spores of P. viticola resulted in a dramatic increase in oxidized glutathione, suggesting the participation of reduced glutathione in S° reduction. In conclusion, we suggest that the fungicidal action of S° is probably related to the oxidation of important sulphydryl groups and not to the competitive interaction between S° and oxygen at the level of the respiratory chain.Key words: elemental sulphur, fungicide, fungi, Neurospora crassa, Phomospis viticola.



2004 ◽  
Vol 17 (4) ◽  
pp. 314-315 ◽  
Author(s):  
Sadhana Khawas ◽  
Dipsikha Panja ◽  
Subrata Laskar


Genome ◽  
1991 ◽  
Vol 34 (4) ◽  
pp. 644-651 ◽  
Author(s):  
Kenneth Koo ◽  
W. Dorsey Stuart

The gene product of the mtr locus of Neurospora crassa is required for the transport of neutral aliphatic and aromatic amino acids via the N system. We have previously cloned three cosmids containing Neurospora DNA that complement the mtr-6(r) mutant allele. The cloned DNAs were tightly linked to restriction fragment length polymorphisms that flank the mtr locus. A 2.9-kbp fragment from one cosmid was subcloned and found to complement the mtr-6(r) allele. Here we report the sequence of the fragment that hybridized to a poly(A)+ mRNA transcript of about 2300 nucleotides. We have identified an 845-bp open reading frame (ORF) having a 59-bp intron as the potential mtr ORF. S1 nuclease analysis of the transcript confirmed the transcript size and the presence of the intron. A second open reading frame was found upstream in the same reading frame as the mtr ORF and appears to be present in the mRNA transcript. The mtr ORF is predicted to encode a 261 amino acid polypeptide with a molecular mass of 28 613 Da. The proposed polypeptide exhibits six potential α-helical transmembrane domains with an average length of 23 amino acids, does not have a signal sequence, and contains amino acid sequence homologous to an RNA binding motif.Key words: sequence, membranes, ribonucleoprotein.







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