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Further Characterization of the Signaling Proteolysis Step in the Aspergillus nidulans pH Signal Transduction Pathway

María M. Peñas, América Hervás-Aguilar, Tatiana Múnera-Huertas, Elena Reoyo, Miguel Á. Peñalva, Herbert N. Arst Jr., Joan Tilburn
María M. Peñas
1Department of Molecular Microbiology and Infection, Imperial College London, The Flowers Building, London SW7 2AZ, United Kingdom
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América Hervás-Aguilar
2Departamento de Microbiología Molecular, Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu, 9, Madrid 28040, Spain
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Tatiana Múnera-Huertas
1Department of Molecular Microbiology and Infection, Imperial College London, The Flowers Building, London SW7 2AZ, United Kingdom
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Elena Reoyo
2Departamento de Microbiología Molecular, Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu, 9, Madrid 28040, Spain
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Miguel Á. Peñalva
2Departamento de Microbiología Molecular, Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu, 9, Madrid 28040, Spain
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Herbert N. Arst Jr.
1Department of Molecular Microbiology and Infection, Imperial College London, The Flowers Building, London SW7 2AZ, United Kingdom
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Joan Tilburn
1Department of Molecular Microbiology and Infection, Imperial College London, The Flowers Building, London SW7 2AZ, United Kingdom
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  • For correspondence: j.tilburn@imperial.ac.uk
DOI: 10.1128/EC.00047-07
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ABSTRACT

The Aspergillus nidulans pH-responsive transcription factor PacC is modulated by limited, two-step proteolysis. The first, pH-regulated cleavage occurs in the 24-residue highly conserved “signaling protease box” in response to the alkaline pH signal. This is transduced by the Pal signaling pathway, containing the predicted calpain-like cysteine protease and likely signaling protease, PalB. In this work, we carried out classical mutational analysis of the putative signaling protease PalB, and we describe 9 missense and 18 truncating loss-of-function (including null) mutations. Mutations in the region of and affecting directly the predicted catalytic cysteine strongly support the deduction that PalB is a cysteine protease. Truncating and missense mutations affecting the C terminus highlight the importance of this region. Analysis of three-hemagglutinin-tagged PalB in Western blots demonstrates that PalB levels are independent of pH and Pal signal transduction. We have followed the processing of MYC3-tagged PacC in Western blots. We show unequivocally that PalB is essential for signaling proteolysis and is definitely not the processing protease. In addition, we have replaced 15 residues of the signaling protease box of MYC3-tagged PacC (pacC900) with alanine. The majority of these substitutions are silent. Leu481Ala, Tyr493Ala, and Gln499Ala result in delayed PacC processing in response to shifting from acidic to alkaline medium, as determined by Western blot analysis. Leu498Ala reduces function much more markedly, as determined by plate tests and processing recalcitrance. Excepting Leu498, this demonstrates that PacC signaling proteolysis is largely independent of sequence in the cleavage region.

  • Copyright © 2007 American Society for Microbiology
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Further Characterization of the Signaling Proteolysis Step in the Aspergillus nidulans pH Signal Transduction Pathway
María M. Peñas, América Hervás-Aguilar, Tatiana Múnera-Huertas, Elena Reoyo, Miguel Á. Peñalva, Herbert N. Arst Jr., Joan Tilburn
Eukaryotic Cell Jun 2007, 6 (6) 960-970; DOI: 10.1128/EC.00047-07

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Further Characterization of the Signaling Proteolysis Step in the Aspergillus nidulans pH Signal Transduction Pathway
María M. Peñas, América Hervás-Aguilar, Tatiana Múnera-Huertas, Elena Reoyo, Miguel Á. Peñalva, Herbert N. Arst Jr., Joan Tilburn
Eukaryotic Cell Jun 2007, 6 (6) 960-970; DOI: 10.1128/EC.00047-07
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KEYWORDS

Aspergillus nidulans
Cysteine Endopeptidases
Fungal Proteins
Hydrogen-Ion Concentration
Signal Transduction
Transcription Factors

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