The N-terminal membrane occupation and recognition nexus domain of Arabidopsis phosphatidylinositol phosphate kinase 1 regulates enzyme activity.
作者： Yang Ju Im , Amanda J. Davis , Imara Y. Perera , Eva Johannes , Nina S. Allen
关键词: N-terminus 、 Cell biology 、 Peptide 、 Phosphatidic acid 、 Kinase activity 、 Phosphatidylinositol 、 Endomembrane system 、 Kinase 、 Phosphatidylinositol phosphate kinases 、 Biology 、 Biochemistry
摘要: The type I B family of phosphatidylinositol phosphate kinases (PIPKs) contain a characteristic region Membrane Occupation and Recognition Nexus (MORN) motifs at the N terminus. These MORN are not found in PIPKs from other eukaryotes. To understand impact additional N-terminal domain on protein function subcellular distribution, we expressed truncated full-length versions AtPIPK1, one member this PIPKs, Escherichia coli tobacco cells grown suspension culture. Deletion (amino acids 1–251) AtPIPK1 increased specific activity remaining C-terminal peptide (ΔMORN) >4-fold eliminated activation by phosphatidic acid (PtdOH). PtdOH could also be mutating Pro396 to Ala (P396A) predicted linker between kinase homology domains. is product-activated binds PtdIns(4,5)P2. Adding back ΔMORN or PtdOH-activated ∼2-fold. Furthermore, expressing vivo plasma membrane PtdInsP activity. When were exposed hyperosmotic stress, redistributed lower phase endomembrane fraction. In addition, endogenous fraction hyperosmotically stressed cells. We conclude that can regulate both distribution enzyme manner sensitive lipid environment.
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