PepJ is a new extracellular proteinase of Aspergillus nidulans

Emri, Tamás; Szilágyi, Melinda; László, K.; M-Hamvas, Márta; Pócsi, István

doi:10.1007/s12223-009-0015-8

Cited by 16 publications

(13 citation statements)

References 22 publications

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“…The spectral counts in WB were comparatively lower than in SBP, even though the activity inhibition was much higher in WB than in SBP, suggesting higher specific activity of metallo proteases present in WB. Alkaline protease AN7962 [43] was the only metallo protease detected in A. nidulans cultures by proteomics. The spectral counts of this protein in WB were two-fold higher than in SBP.…”

Section: Resultsmentioning

confidence: 99%

A genomic survey of proteases in Aspergilli

et al. 2014

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BackgroundProteases can hydrolyze peptides in aqueous environments. This property has made proteases the most important industrial enzymes by taking up about 60% of the total enzyme market. Microorganisms are the main sources for industrial protease production due to their high yield and a wide range of biochemical properties. Several Aspergilli have the ability to produce a variety of proteases, but no comprehensive comparative study has been carried out on protease productivity in this genus so far.ResultsWe have performed a combined analysis of comparative genomics, proteomics and enzymology tests on seven Aspergillus species grown on wheat bran and sugar beet pulp. Putative proteases were identified by homology search and Pfam domains. These genes were then clusters based on orthology and extracellular proteases were identified by protein subcellular localization prediction. Proteomics was used to identify the secreted enzymes in the cultures, while protease essays with and without inhibitors were performed to determine the overall protease activity per protease class. All this data was then integrated to compare the protease productivities in Aspergilli.ConclusionsGenomes of Aspergillus species contain a similar proportion of protease encoding genes. According to comparative genomics, proteomics and enzymatic experiments serine proteases make up the largest group in the protease spectrum across the species. In general wheat bran gives higher induction of proteases than sugar beet pulp. Interesting differences of protease activity, extracellular enzyme spectrum composition, protein occurrence and abundance were identified for species. By combining in silico and wet-lab experiments, we present the intriguing variety of protease productivity in Aspergilli.Electronic supplementary materialThe online version of this article (doi:10.1186/1471-2164-15-523) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

A genomic survey of proteases in Aspergilli

et al. 2014

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“…Other genes with documented functions that showed differential expression in response to carbon starvation in the xprGΔ1 mutant include two genes encoding extracellular proteases ( prtA and pepJ ) which are known to be expressed during starvation 5, 40, 41 . The expression of prtA in response to carbon or nitrogen starvation has been shown to be XprG-dependent 6 .…”

Section: Resultsmentioning

confidence: 99%

A p53-like transcription factor similar to Ndt80 controls the response to nutrient stress in the filamentous fungus, Aspergillus nidulans

Katz

Braunberger

et al. 2013

F1000Res

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The Aspergillus nidulans xprG gene encodes a putative transcriptional activator that is a member of the Ndt80 family in the p53-like superfamily of proteins. Previous studies have shown that XprG controls the production of extracellular proteases in response to starvation. We undertook transcriptional profiling to investigate whether XprG has a wider role as a global regulator of the carbon nutrient stress response. Our microarray data showed that the expression of a large number of genes, including genes involved in secondary metabolism, development, high-affinity glucose uptake and autolysis, were altered in an xprG Δ null mutant. Many of these genes are known to be regulated in response to carbon starvation. We confirmed that sterigmatocystin and penicillin production is reduced in xprG - mutants. The loss of fungal mass and secretion of pigments that accompanies fungal autolysis in response to nutrient depletion was accelerated in an xprG1 gain-of-function mutant and decreased or absent in an xprG - mutant. The results support the hypothesis that XprG plays a major role in the response to carbon limitation and that nutrient sensing may represent one of the ancestral roles for the p53-like superfamily. Disruption of the AN6015 gene, which encodes a second Ndt80-like protein, showed that it is required for sexual reproduction in A. nidulans.

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“…4). The deletion of engA decreased mRNA accumulation of the genes pepJ (encoding the metalloproteinase PepJ; Emri et al. 2009), prtA (encoding the serine proteinase PrtA; Katz et al.…”

Section: Resultsmentioning

confidence: 99%

The extracellular β-1,3-endoglucanase EngA is involved in autolysis of Aspergillus nidulans

Szilágyi

Kwon

Dorogi

et al. 2010

Journal of Applied Microbiology

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Aims: To elucidate the roles of the b-1,3-endoglucanase EngA in autolysis of the filamentous fungus Aspergillus nidulans and to identify the common regulatory elements of autolytic hydrolases. Methods and Results: A b-1,3-endoglucanase was purified from carbonstarving cultures of A. nidulans. This enzyme is found to be encoded by the engA gene (locus ID: AN0472.3). Functional and gene-expression studies demonstrated that EngA is involved in the autolytic cell wall degradation resulting from carbon starvation of the fungus. Moreover, regulation of engA is found to be dependent on the FluG ⁄ BrlA asexual sporulation signalling pathway in submerged culture. The deletion of either engA or chiB (encoding an endochitinase) caused highly reduced production of hydrolases in general. Conclusions: The b-1,3-endoglucanase EngA plays a pivotal role in fungal autolysis, and activities of both EngA and ChiB are necessary to orchestrate the expression of autolytic hydrolases. The production of cell wall-degrading enzymes was coordinately controlled in a highly sophisticated and complex manner. Significance and Impact of the Study: No information was available on the autolytic glucanase(s) of the euascomycete A. nidulans. This study demonstrates that EngA is a key element in fungal autolysis, and normal activities of both EngA and ChiB are crucial for balanced production of hydrolases. in nutrition acquisition and morpholytic events including autolysis (Pitson et al. 1993;Adams 2004;Martin et al. 2007). These glucanases are regulated mainly by induction and carbon catabolite repression, although nitrogen catabolite repression and constitutive enzyme production have also been reported (Pitson et al. 1993;Martin et al. 2007). Because these enzymes are extremely valuable in brewing, wine making, food and feed productions as well as in chemical analyses and syntheses, the factors influencing their fermentation yields have been studied extensively (Jayus et al. 2002(Jayus et al. , 2005Martin et al. 2007).It is important to note that while circumstantial evidence indicating a potential involvement of extracellular b-1,3-glucanases in the autolysis of filamentous fungi has been obtained in the last decades (Lahoz et al. 1976(Lahoz et al. , 1983Santos et al. 1979;Gó mez-Alarcó n et al. 1986;Copa-Patiño et al. 1989;Nuero et al. 1993), this hypothesized physiological function has remained yet to be verified by functional characterization of the corresponding gene(s). To the best of our knowledge, only the engl1 gene encoding a cell wall-associated b-1,3-endoglucanase has been disrupted in Aspergillus fumigatus, which resulted in no clear phenotypic changes (Mouyna et al. 2002;Martin et al. 2007). On the contrary, the involvement of the A. nidulans extracellular endochitinase ChiB in the autolytic cell wall-degradation process has been demonstrated by several research groups (Yamazaki et al. 2007;Pó csi et al. 2009;Shin et al. 2009).In this study, we present data on the purification and characterization of an extracellular autolyt...

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PepJ is a new extracellular proteinase of Aspergillus nidulans

Cited by 16 publications

References 22 publications

A genomic survey of proteases in Aspergilli

A genomic survey of proteases in Aspergilli

A p53-like transcription factor similar to Ndt80 controls the response to nutrient stress in the filamentous fungus, Aspergillus nidulans

The extracellular β-1,3-endoglucanase EngA is involved in autolysis of Aspergillus nidulans

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