The Asp1 pyrophosphatase from S. pombe hosts a [2Fe-2S]2+ cluster in vivo
Rosenbach H, Walla E, Cutsail GE, Birrell JA, Pascual-Ortiz M, Debeer S, Fleig U, Span I (2021)
Publication Type: Journal article
Publication year: 2021
Journal
Book Volume: 26
Pages Range: 93-108
Journal Issue: 1
DOI: 10.1007/s00775-020-01840-w
Abstract
The Schizosaccharomyces pombe Asp1 protein is a bifunctional kinase/pyrophosphatase that belongs to the highly conserved eukaryotic diphosphoinositol pentakisphosphate kinase PPIP5K/Vip1 family. The N-terminal Asp1 kinase domain generates specific high-energy inositol pyrophosphate (IPP) molecules, which are hydrolyzed by the C-terminal Asp1 pyrophosphatase domain (Asp1365−920). Thus, Asp1 activities regulate the intracellular level of a specific class of IPP molecules, which control a wide number of biological processes ranging from cell morphogenesis to chromosome transmission. Recently, it was shown that chemical reconstitution of Asp1371−920 leads to the formation of a [2Fe-2S] cluster; however, the biological relevance of the cofactor remained under debate. In this study, we provide evidence for the presence of the Fe–S cluster in Asp1365−920 inside the cell. However, we show that the Fe–S cluster does not influence Asp1 pyrophosphatase activity in vitro or in vivo. Characterization of the as-isolated protein by electronic absorption spectroscopy, mass spectrometry, and X-ray absorption spectroscopy is consistent with the presence of a [2Fe-2S]2+ cluster in the enzyme. Furthermore, we have identified the cysteine ligands of the cluster. Overall, our work reveals that Asp1 contains an Fe–S cluster in vivo that is not involved in its pyrophosphatase activity.
Authors with CRIS profile
Involved external institutions
Heinrich-Heine-Universität Düsseldorf
Germany (DE)
Max-Planck-Institut für Chemische Energiekonversion (MPI CEC) / Max-Planck-Institute for Chemical Energy Conversion
Germany (DE)
Universidad Cardenal Herrera
Spain (ES)
Germany (DE)
Max-Planck-Institut für Chemische Energiekonversion (MPI CEC) / Max-Planck-Institute for Chemical Energy Conversion
Germany (DE)
Universidad Cardenal Herrera
Spain (ES)
How to cite
APA:
Rosenbach, H., Walla, E., Cutsail, G.E., Birrell, J.A., Pascual-Ortiz, M., Debeer, S.,... Span, I. (2021). The Asp1 pyrophosphatase from S. pombe hosts a [2Fe-2S]2+ cluster in vivo. Journal of Biological Inorganic Chemistry, 26(1), 93-108. https://doi.org/10.1007/s00775-020-01840-w
MLA:
Rosenbach, Hannah, et al. "The Asp1 pyrophosphatase from S. pombe hosts a [2Fe-2S]2+ cluster in vivo." Journal of Biological Inorganic Chemistry 26.1 (2021): 93-108.
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