Isolation and analysis of the Penicillium chrysogenum phoA gene encoding a secreted phosphate-repressible acid phosphatase

Haas, Hubertus; Redl, Bernhard; Friedlin, Ernst; Stöffler, Georg

doi:10.1016/0378-1119(92)90680-n

Cited by 43 publications

(21 citation statements)

References 20 publications

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“…Phosphaterepressed acid phosphatases have been described in S. cerevisiae (Vogel & Hinnen, 1990), A. niger (MacRae et al, 1988 and P. chrysogenum (Haas et al, 1991(Haas et al, , 1992. Phosphate is essential for the growth of all fungi (Jennings, 1995), and A. fumigatus was unable to grow at a P i concentration lower than 10 µM.…”

Section: Discussionmentioning

confidence: 99%

“…4), namely acid phosphatase P34724 of Aspergillus niger (62 % identity ; Ehrlich, 1994), acid phosphatase P37274 of Penicillium chrysogenum (60 % identity ; Haas et al, 1991Haas et al, , 1992 and acid phosphatases JC7179 and P08540 of Kluyveromyces marxianus (56 and 51 % identity, respectively ; Yoda et al, 2000). AfPhoAp also showed a lower level of identity with bacterial acid phosphatases, such as E70842 of Mycobacterium tuberculosis (Saleh & Belisle, 2000 RHGXRXP motif typical of many phosphatase enzymes (Van Etten et al, 1991) was not present in any of these phosphatases, but histidine 214 and aspartic acid 215, conserved in all of these proteins, could be part of the catalytic active site (Ostanin et al, 1992).…”

Section: Molecular Characterization Of the 80 Kda Cell-wallassociatedmentioning

confidence: 99%

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Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus The GenBank accession number for the A. fumigatus PHOA sequence reported in this paper is AF462065.

et al. 2002

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In the filamentous fungus Aspergillus fumigatus, the vast majority of the cellwall-associated proteins are secreted proteins that are in transit in the cell wall. These proteins can be solubilized by detergents and reducing agents. Incubation of a SDS/β-mercaptoethanol-treated cell-wall extract with various recombinant enzymes that hydrolyse cell-wall polysaccharides resulted in the release of a unique protein in minute amounts only after incubation of the cell wall in the presence of 1,3-β-glucanase. Sequence analysis and biochemical studies showed that this glycoprotein, with an apparent molecular mass of 80 kDa, was an acid phosphatase (PhoAp) that was active on both phosphate monoesters and phosphate diesters. PhoAp is a glycosylphosphatidylinositolanchored protein that was recovered in the culture filtrate and cell-wall fraction of A. fumigatus after cleavage of its anchor. It is also a phosphaterepressible acid phosphatase. The absence of PhoAp from a phosphate-rich medium was not associated with a reduction in fungal growth, indicating that this cell-wall-associated protein does not play a role in the morphogenesis of A. fumigatus.

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Section: Discussionmentioning

confidence: 99%

Section: Molecular Characterization Of the 80 Kda Cell-wallassociatedmentioning

confidence: 99%

Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus The GenBank accession number for the A. fumigatus PHOA sequence reported in this paper is AF462065.

et al. 2002

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“…Five putative acid phosphatase genes and 8 phytase genes were found. It was considered that the expression of the putative acid phosphatase genes might be repressed by the phosphate from phytate in soybean because these genes are homologous to the phosphate repressible acid phosphatase gene from Aspergillus niger (MacRae et al, 1988) and Penicillium chrysogenum (Hass et al, 1992). Among the remaining candidate genes, the gene (NITE DOGAN ID: AO090023000692) with the highest similarity to the well-characterized A. niger phyA gene (van Hartingsveldt et al, 1993) was chosen.…”

Section: Resultsmentioning

confidence: 99%

Disruption and Overexpression of Acid Phosphatase Gene (aphA) from a Miso Koji Mold, Aspergillus oryzae KBN630, and Characterization of the Gene Product

Yoshino-Yasuda

Hasegawa

Iga³

et al. 2012

FSTR

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An acid phosphatase gene (aphA gene) from an industrial miso koji mold strain, A. oryzae KBN630, was disrupted by using the recently developed homologous gene replacement system for this strain. The aphA gene disruption did not affect growth on steamed soybean. Acid phosphatase production decreased by approximately 20% in the aphA gene disruptants compared with that of the wild-type strain. Utilizing the promoter of the A. oryzae TEF1 gene, AphA expressed in A. oryzae was successfully secreted into the culture medium. AphA had a molecular mass of 58.0 to 65.0 kDa, a pH optimum of 4.0, and a temperature optimum of 40℃. AphA had the ability to release inorganic phosphate from GMP and IMP. This is the first report to show directly that an A. oryzae acid phosphatase has the ability to hydrolyze GMP and IMP.

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“…Indeed, this motif is also located in the promoter region of the pH-regulated acid phosphatase phoA gene of P. chrysogenum (40).…”

Section: That Have Been Identified In a Nidulans [Consensus Sequencementioning

confidence: 97%

Molecular Control of Expression of Penicillin Biosynthesis Genes in Fungi: Regulatory Proteins Interact with a Bidirectional Promoter Region

Martı́n

2000

J Bacteriol

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Isolation and analysis of the Penicillium chrysogenum phoA gene encoding a secreted phosphate-repressible acid phosphatase

Cited by 43 publications

References 20 publications

Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus The GenBank accession number for the A. fumigatus PHOA sequence reported in this paper is AF462065.

Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus The GenBank accession number for the A. fumigatus PHOA sequence reported in this paper is AF462065.

Disruption and Overexpression of Acid Phosphatase Gene (aphA) from a Miso Koji Mold, Aspergillus oryzae KBN630, and Characterization of the Gene Product

Molecular Control of Expression of Penicillin Biosynthesis Genes in Fungi: Regulatory Proteins Interact with a Bidirectional Promoter Region

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