Functional characterisation of parvulin-type peptidyl prolyl cis-trans isomerase, PinA in Dictyostelium discoideum.
Pin1-type parvulins are unique among PPIases that can catalyse an otherwise slow cis-trans isomerisation of phosphorylated peptide bond preceding proline in target proteins. This prolyl isomerisation process can regulate activity, stability and localisation of target proteins and thus control cellular processes like eukaryotic cell proliferation, cell cycle progression and gene regulation. Towards understanding the function of Pin1-type prolyl isomerisation in Dictyostelium discoideum, a slime mould with distinct growth and developmental phases, we identified PinA as a novel Pin1-type parvulin by its ability to complement the temperature sensitivity phenotype associated with a mutation in ESS1 in S. cerevisiae. In D. discoideum, pinA is temporally and spatially regulated during growth and development. PinA is both nuclear as well as cytoplasmic in the growing cells. We further show that loss of pinA (pinA-) leads to decreased growth rate, reduced spore formation and abnormal prespore-prestalk patterning. We conclude that PinA is required for normal growth as well as development in D. discoideum.
Department of Genetics, University of Delhi, South Campus, Benito Juarez Road, New Delhi, 110021, India.
Nemneineng
N
Haokip
Department of Genetics, University of Delhi, South Campus, Benito Juarez Road, New Delhi, 110021, India. Electronic address: aruna.naorem@south.du.ac.in.
Aruna
A
Naorem
D001665:Binding Sites; D002454:Cell Differentiation / Q000502:physiology; D049109:Cell Proliferation / Q000502:physiology*; D048429:Cell Size; D004023:Dictyostelium / Q000166:cytology* / Q000201:enzymology*; D004789:Enzyme Activation; D019696:Peptidylprolyl Isomerase / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D013379:Substrate Specificity
D019696:Peptidylprolyl Isomerase
Dictyostelium discoideum; FHA domain; Parvulin; Peptidyl prolyl cis-trans isomerase; Pin1-type PPlase; PinA