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PLANT PHYSIOLOGY , Vol 102, Issue 1 133-138, Copyright © 1993 by American Society of Plant Biologists
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MOLECULAR BIOLOGY AND GENE REGULATION |
Molecular Characterization of a Polygalacturonase Inhibitor from Pyrus communis L. cv Bartlett
H. U. Stotz, ALT. Powell, S. E. Damon, L. C. Greve, A. B. Bennett and J. M. Labavitch
Departments of Pomology (H.U.S., L.C.G., J.M.L.) and Vegetable Crops (A.L.T.P., S.E.D., A.B.B.), University of California, Davis, California 95616
A polygalacturonase inhibitor glycoprotein with an apparent molecular mass
of 43 kD was purified from pear (Pyrus communis L. cv Bartlett) fruit.
Chemical deglycosylation of this protein decreased the molecular mass to 34
kD. Gas chromatographic analysis suggests that N-linked glycosylation
accounts for the majority of sugar moieties. Partial amino acid sequence
analysis of the purified polygalacturonase inhibitor protein provided
information used to amplify a corresponding cDNA by polymerase chain
reactions. Multiple cloned products of these reactions were sequenced and
the same open reading frame was identified in all of the products. It
encodes a 36.5-kD polypeptide containing the amino acid sequences
determined by protein sequencing and predicts a putative signal sequence of
24 amino acids and seven potential N-glycosylation sites. The expression of
polygalacturonase inhibitor is regulated in a tissue-specific manner.
Activity and mRNA level were much higher in fruit than in flowers or
leaves.
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