Endopolyphosphatase in Saccharomyces cerevisiae undergoes post‐translational activations to produce short‐chain polyphosphates
- 24 February 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (9) , 2014-2018
- https://doi.org/10.1016/j.febslet.2005.02.032
Abstract
Endopolyphosphatase (Ppn), responsible for cleavage of long chain inorganic polyphosphate (poly P) of several hundred residues to generate progressively shorter chains, has been identified in mammalian cells and purified from Saccharomyces cerevisiae. Disruption of the encoding gene, PHM5, in S. cerevisiae resulted in a mutant that showed limited growth and failure to survive in a minimal medium. The limited digestion products of the yeast enzyme Ppn1 judged to be P(3) and P(60) have now, with the homogeneous enzyme and improved separation methods, been demonstrated to be P(i) and P(3). Ppn1, a homotetramer of a 35-kDa subunit, is of vacuolar origin and requires protease activation of a 78 kDa (674-aa) precursor polypeptide (prePpn1). The protease-processed Ppn1 has been purified 3800-fold to homogeneity and the protease cleavage sites determined. Both termini of prePpn1 and the post-translational modification of N-glycosylations are essential for the protease-mediated maturation of Ppn1.Keywords
This publication has 21 references indexed in Scilit:
- The Ubiquitin Ligase Rsp5p is Required for Modification and Sorting of Membrane Proteins into Multivesicular BodiesTraffic, 2004
- A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodiesNature Cell Biology, 2002
- Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targetingThe EMBO Journal, 2001
- The endopolyphosphatase gene: Essential in Saccharomyces cerevisiaeProceedings of the National Academy of Sciences, 2001
- N-Glycosylation of yeast, with emphasis onCandida albicansMedical Mycology, 2001
- New Components of a System for Phosphate Accumulation and Polyphosphate Metabolism inSaccharomyces cerevisiaeRevealed by Genomic Expression AnalysisMolecular Biology of the Cell, 2000
- Polar Transmembrane Domains Target Proteins to the Interior of the Yeast VacuoleMolecular Biology of the Cell, 2000
- Polyphosphate kinase is essential for biofilm development, quorum sensing, and virulence of Pseudomonas aeruginosaProceedings of the National Academy of Sciences, 2000
- Inorganic Polyphosphate: A Molecule of Many FunctionsAnnual Review of Biochemistry, 1999
- Inorganic polyphosphate and the induction of rpoS expressionProceedings of the National Academy of Sciences, 1997