Characterization of a fission yeast P5-type ATPase homologue that is essential for Ca2+/Mn2+ homeostasis in the absence of P2+-type ATPases

Abstract

In the fission yeast Schizosaccharomyces pombe, three P-type ATPases, namely Cta4p, Pmrlp, and Pmclp, have been shown to be essential for Ca 2+ homeostasis and are required for specific cellular functions as well. Here, we show that the simultaneous deletion of pmc1+ and SPAC29A4.19c, which encodes a putative P5+type ATPase, causes a hypersensitive growth to either high concentrations of Ca2+ in a medium, or the antiarrhythmic drug amiodarone, which has been known to cause a disruption of Ca2+ homeostasis. On the other hand, simultaneous deletion of pmr1+ and SPAC29A4.19c causes a hypersensitive growth to Mn2+ depletion in a medium. The green fluorescent protein-tagged SPAC29A4.19c protein reveals a typical localization pattern of the Golgi proteins, but the SPAC29A4.19c protein is not exchangeable in function with Pmrlp, which is required for Ca2+/Mn2+ homeostasis in secretory pathways. These results suggest that the putative P5+-type ATPase encoded by SPAC29A4.19c is essential for Ca2+ and Mn 2+ homeostasis in the absence of P2-type ATPases, Pmclp or Pmrlp, respectively. According to the precedent nomenclature of calcium/cation transporting ATPase in fission yeast, SPAC29A4.19 was named cta5+ in this study.