Abstract：
:Polygalacturonase inhibiting proteins (PGIPs) are members of the leucine rich repeat family of proteins, involved in plant defense against fungal pathogens. PGIPs exhibit a remarkable degree of specificity in terms of their ability to bind and inhibit their target molecules, the endopolygalacturonases (EPGs). This specificity has been attributed for certain EPG/PGIP combinations to differences in primary sequence, but this explanation is unable to account for the full range of binding and inhibitory activities observed. In this paper, we have fully characterized the glycosylation on the PGIP derived from Pyrus communis and demonstrated, using a combination of PNGaseF and PNGaseA in (18)O-water, that the Pyrus communis PGIP utilizes all seven potential sites of N-linked glycosylation. Further, we demonstrate that certain sites appear to be modified only by glycans bearing alpha3-linked core fucosylation, while others are occupied by a mixture of fucosylated and nonfucosylated glycans. Modeling of the carbohydrates onto a homologous structure of PGIP indicates potential roles for glycosylation in mediating the interactions of PGIPs with EPGs.
journal_name
J Proteome Resjournal_title
Journal of proteome researchauthors
Lim JM,Aoki K,Angel P,Garrison D,King D,Tiemeyer M,Bergmann C,Wells Ldoi
10.1021/pr800855fsubject
Has Abstractpub_date
2009-02-01 00:00:00pages
673-80issue
2eissn
1535-3893issn
1535-3907pii
10.1021/pr800855fjournal_volume
8pub_type
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