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Yarrowia lipolytica pp 77–97Cite as

Acid and Alkaline Extracellular Proteases of Yarrowia lipolytica

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Part of the book series: Microbiology Monographs ((MICROMONO,volume 25))

Abstract

XPR2 and AXP1, coding for alkaline (AEP) and acid (AXP) extracellular proteases, have been sequenced for several strains. For XPR2, the three sequenced strains are not closely related and produce significantly different levels of AEP, yet the coding sequences are identical, and there is only a single nucleotide difference in one promoter suggesting that host physiology, not promoter differences, determines AEP production. The possibility that pro-mAEP forms a dimer that can inhibit mature AEP (mAEP) proteolytic activity in trans is examined. AXP contains a predicted signal sequence and a 44 amino acid prepro-region. Activation involves pH-dependent autoprocessing that occurs extracellularly. XPR2 UAS1 and UAS2 promoter elements have been identified and their roles in regulation explored. Cis-sequences and Rim pathway components involved in pH regulation of the proteases have been discovered and characterized. YlOPT1 and YLSSY5 are in a signaling pathway(s) regulating AXP1 and XPR2, perhaps by sensing amino acids. Both pepsin-like (30 potentially secreted members) and subtilisin-like (16 potentially secreted members) gene families have undergone lineage-specific expansion compared to other yeast and filamentous fungi. To determine if expression of secretory pathway components is regulated in response to secretory demand, rapid AEP induction conditions and XPR2 multicopy strains were developed. Changes in genomic transcription were measured when growth started to slow after AEP induction. For secretory pathway components, mostly repression was found. Possibly, their induction had occurred by the control time point, and the turning off of this short-term response at later time points appeared as repression.

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Authors and Affiliations

  1. Department of Food Science and Technology, University of California, One Shields Avenue, Davis, CA, 95616, USA

    David Ogrydziak

  2. Institute of Marine Resources, University of California, Davis, CA, USA

    David Ogrydziak

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  1. David Ogrydziak
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Correspondence to David Ogrydziak .

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Editors and Affiliations

  1. TU Dresden Inst. Mikrobiologie, Dresden, Sachsen, Germany

    Gerold Barth

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Ogrydziak, D. (2013). Acid and Alkaline Extracellular Proteases of Yarrowia lipolytica . In: Barth, G. (eds) Yarrowia lipolytica. Microbiology Monographs, vol 25. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-38583-4_2

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