On the Mechanism by which Alkaline pH Prevents Expression of an Acid-Expressed Gene

Espeso, Eduardo A.; Arst, Herbert N.

doi:10.1128/mcb.20.10.3355-3363.2000

Cited by 95 publications

(81 citation statements)

References 40 publications

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“…Through binding to a 59-GCCARG-39 consensus DNA sequence, PacC is considered an activator of alkalineexpressed genes (Penalva & Arst, 2002) and it was shown to repress one acid-expressed gene (Espeso & Arst, 2000). Other acid-expressed genes, however, lack the consensus PacC binding site upstream of their coding sequence (Sarkar et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea

et al. 2009

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During pathogenesis, the ascomycete Botrytis cinerea secretes a range of cell-wall-degrading enzymes such as polygalacturonases, glucanases and proteases. We report the identification of a new member of the G1 family of proteases, BcACP1, which is secreted by B. cinerea during infection. The production of BcACP1 correlates with the acidification of the plant tissue, and transcriptional analysis of the Bcacp1 gene showed that it is only expressed under acidic growth conditions. Using a transcriptional reporter system, we showed that pH regulation of Bcacp1 is not mediated by the canonical PacC transcription factor binding site. Like other G1 proteases, BcACP1 is produced as a pro-enzyme. Trapping of the zymogen form allowed investigation of its maturation process. Evidence is presented for an autocatalytic proteolysis of the enzyme that is triggered by acidic pH. Environmental pH therefore controls Bcacp1 production at both the transcriptional and post-translational level.

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Section: Discussionmentioning

confidence: 99%

pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea

et al. 2009

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“…At alkaline pH, the transcription factor PacC acts as both an activator of alkali-expressed genes and a repressor of acid-expressed genes through the same consensus promoter recognition motif (Espeso & Arst, 2000;Tilburn et al, 1995). In F. verticillioides, fumonisin production, which occurs at acidic pH, is likely to be negatively regulated by the PacC homologue (Flaherty et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Low pH regulates the production of deoxynivalenol by Fusarium graminearum

et al. 2009

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Fusarium graminearum, which causes the globally important head blight disease of wheat, is responsible for the production of the harmful mycotoxin deoxynivalenol (DON) in infected grain. The production of DON by F. graminearum occurs at much higher levels during infection than during axenic growth, and it is therefore important to understand how DON production is regulated in the fungus. Recently, we have identified amines as potent inducers of in vitro DON production in F. graminearum. Although amines strongly induced expression of the key DON biosynthesis gene TRI5 and DON production to levels equivalent to those observed during infection, the timing of this induction suggested that other factors are also likely to be important for the regulation of DON biosynthesis. Here we demonstrate that low extracellular pH both promotes and is required for DON production in F. graminearum. A combination of low pH and amines results in significantly enhanced expression of the TRI5 gene and increased DON production during axenic growth. A better understanding of DON production in F. graminearum would have implications in developing future toxin management strategies.

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“…This pal pathway is activated by alkaline ambient pH, which leads to the 2-step proteolytic conversion of the 72-kDa PacC 72 translation product into the 53 kDa committed intermediate PacC 53 and the 27-kDa final product PacC 27 (10 -12). PacC 27 is a transcriptional activator of alkaline-expressed genes and a repressor of acid-expressed genes (13,14). The alkaline ambient pH-dependent conversion of PacC 72 into PacC 53 is almost certainly catalyzed by the calpain-like cysteine protease PalB (10,15,16) (see Refs.…”

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confidence: 99%

Physiological Involvement in pH Signaling of Vps24-mediated Recruitment of Aspergillus PalB Cysteine Protease to ESCRT-III

Rodríguez-Galán

Galindo

Hervás-Aguilar

et al. 2009

Journal of Biological Chemistry

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On the Mechanism by which Alkaline pH Prevents Expression of an Acid-Expressed Gene

Cited by 95 publications

References 40 publications

pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea

pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea

Low pH regulates the production of deoxynivalenol by Fusarium graminearum

Physiological Involvement in pH Signaling of Vps24-mediated Recruitment of Aspergillus PalB Cysteine Protease to ESCRT-III

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