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|Title: ||Isolation of papaya carboxy-terminal protease CDNA clone during ripening|
|Authors: ||Roohaida O.|
Chong, H. L.
|Issue Date: ||2004|
|Publisher: ||Malaysian Society of Plant Physiology|
|Citation: ||Advances in plant science: Proceedings of the 15th Malaysian Society of Plant Physiology conference: Port Dickson, Negeri Sembilan (Malaysia), 14-16 Sep, 2004, p. 234-239|
|Series: ||Transactions of the Malaysian Society of Plant Physiology|
|Abstract: ||A novel type of serine protease with a Ser/Lys catalytic dyad, is responsible for the C-terminal processing of precursor Dl protein (pDl) of the photosystem II reaction center, a process that is indispensable for the integration of water-splitting machinery in photosynthesis. A papaya cDNA clone coding for a carboxy terminal protease has been isolated from a ripening papaya cDNA library. The expected amino acid sequence shared homology with carboxy-terminal protease gene from Arabidopsis thaliana, Spinacia oleracea and Scenedesmus obliquus which may be involved in removal of carboxy-terminal extension of the D1 protein in photosystem II (PSII). Subsequent sequence comparisons with other plant cDNA sequences showed that the papaya cDNA clone aligned to the middle part of other plant proteases hence indicating truncation at the 5'-end of the clone. Further analysis of the papaya protease sequence showed presence of the catalytic dyad Ser/Lys, a feature common to this enzyme family.|
|Appears in Collections:||Publications|
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