Protease inhibitor studies and cloning of a serine carboxypeptidase cDNA from germinating seeds of pea (Pisum sativum L.).
The nature of the proteolytic activity found within the germinating pea (Pisum sativum) seed, 4 days from the initiation of imbibition, was determined by the use of specific protease inhibitors. These studies have shown most of the activity to belong to metallo or metal-activated and serine proteases. In order to investigate further the serine protease activity, a pea cotyledon germination cDNA library was, therefore, screened with a wheat cDNA (2437) [Baulcombe, D.C., Barker, R.F. & Jarvis, M.G. (1987) J. Biol. Chem. 262, 13726-13735] which had extensive similarity to the yeast serine carboxypeptidase Y gene. A positive cDNA clone (pNY551) was obtained which had extensive similarity to the four carboxypeptidases, Arabidopsis thaliana carboxypeptidase Y-like protein, rice serine carboxypeptidase III, barley serine carboxypeptidase III and wheat serine carboxypeptidase III precursor. Northern-blot analysis showed mRNA homologous to pNY551 to be expressed in late developmental pea seed and again during germination.
Jones
C G
CG
Department of Physiology and Environmental Science, University of Nottingham, Loughborough, UK.
Lycett
G W
GW
Tucker
G A
GA
D000595:Amino Acid Sequence; D002268:Carboxypeptidases / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D018076:DNA, Complementary; D018525:Germination; D008969:Molecular Sequence Data; D018532:Pisum sativum / Q000201:enzymology* / Q000502:physiology; D011480:Protease Inhibitors / Q000494:pharmacology*
D018076:DNA, Complementary; D011480:Protease Inhibitors; D002268:Carboxypeptidases; C022633:serine carboxypeptidase