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Identification of the site on potato carboxypeptidase inhibitor that is phosphorylated by plant calcium-dependent protein kinase






Plant Science (Shannon) 114(1): 45-51

Identification of the site on potato carboxypeptidase inhibitor that is phosphorylated by plant calcium-dependent protein kinase

Potato (Solanum tuberosum) carboxypeptidase inhibitor (PCI) is phosphorylated by wheat Ca-2+-dependent protein kinase (CDPK). While the K-m of PCI for CDPK is high, the rates of phosphorylation of PCI by plant CDPK are also very high in relation to phosphorylation of the histone III-S preparation, an excellent substrate for plant CDPKs. Analysis of intact PCI and of HPLC-resolved chymotryptic fragments of (32P)phosphoPCI (phosphorylated by plant CDPK) by electrospray ionization mass spectrometry (ESMS) confirmed the sequences of three PCI variants, PCIA, PCIB and PCIC. PCIB (4276.75 Da), PCIA (4148.62 Da) and PCIC (3900.38 Da) have differing N-terminal residues, namely lt EQHA-(PCIB), lt EHA-(PCIA) and A-(PCIC) but the remaining sequences are identical. PCI is phosphorylated by plant CDPK on a single exposed site, namely the Ser, corresponding to Ser-27, Ser-29 and Ser-30 of pCIC, PCIA and PCIB, respectively. This phosphorylatable Ser is located within the CWNSARTC sequence and is associated with a Ser-X-Basic motif found with a number of other plant CDPK phosphorylation sites. The phosphorylatable Ser is located on an exposed loop at a secondary point of interaction of PCI with carboxypeptidase.

Accession: 002863914

DOI: 10.1016/0168-9452(95)04307-1

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