Protein Phosphatase Ppz1 Is Not Regulated by a Hal3-Like Protein in Plant Pathogen Ustilago maydis
Ppz enzymes are type-1 related Ser/Thr protein phosphatases that are restricted to fungi. In and other fungi, Ppz1 is involved in cation homeostasis and is regulated by two structurally-related inhibitory subunits, Hal3 and Vhs3, with Hal3 being the most physiologically relevant. Remarkably, Hal3 an...
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Veröffentlicht in: | International journal of molecular sciences 2019-08, Vol.20 (15), p.3817 |
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Zusammenfassung: | Ppz enzymes are type-1 related Ser/Thr protein phosphatases that are restricted to fungi. In
and other fungi, Ppz1 is involved in cation homeostasis and is regulated by two structurally-related inhibitory subunits, Hal3 and Vhs3, with Hal3 being the most physiologically relevant. Remarkably, Hal3 and Vhs3 have moonlighting properties, as they participate in an atypical heterotrimeric phosphopantothenoyl cysteine decarboxylase (PPCDC), a key enzyme for Coenzyme A biosynthesis. Here we identify and functionally characterize Ppz1 phosphatase (UmPpz1) and its presumed regulatory subunit (UmHal3) in the plant pathogen fungus
. UmPpz1 is not an essential protein in
and, although possibly related to the cell wall integrity pathway, is not involved in monovalent cation homeostasis. The expression of UmPpz1 in
Ppz1-deficient cells partially mimics the functions of the endogenous enzyme. In contrast to what was found in
and
, UmPpz1 is not a virulence determinant. UmHal3, an unusually large protein, is the only functional PPCDC in
and, therefore, an essential protein. However, when overexpressed in
or
, UmHal3 does not reproduce Ppz1-inhibitory phenotypes. Indeed, UmHal3 does not inhibit UmPpz1 in vitro (although ScHal3 does). Therefore, UmHal3 might not be a moonlighting protein. |
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ISSN: | 1422-0067 1661-6596 1422-0067 |
DOI: | 10.3390/ijms20153817 |