Open Access. Powered by Scholars. Published by Universities.®

Digital Commons Network

Open Access. Powered by Scholars. Published by Universities.®

Articles 1 - 2 of 2

Full-Text Articles in Entire DC Network

Pmr6, A Pectate Lyase–Like Gene Required For Powdery Mildew Susceptibility In Arabidopsis, John P. Vogel, Ted K. Raab, Celine Schiff, Shauna C. Somerville Sep 2002

Pmr6, A Pectate Lyase–Like Gene Required For Powdery Mildew Susceptibility In Arabidopsis, John P. Vogel, Ted K. Raab, Celine Schiff, Shauna C. Somerville

Ted K. Raab

The plant genes required for the growth and reproduction of plant pathogens are largely unknown. In an effort to identify these genes, we isolated Arabidopsis mutants that do not support the normal growth of the powdery mildew pathogen Erysiphe cichoracearum. Here, we report on the cloning and characterization of one of these genes, PMR6. PMR6 encodes a pectate lyase-like protein with a novel C-terminal domain. Consistent with its predicted gene function, mutations in PMR6 alter the composition of the plant cell wall, as shown by Fourier transform infrared spectroscopy. pmr6-mediated resistance requires neither salicylic acid nor the ability to perceive …


Galactose-Binding Lectin From The Seeds Of Champedak (Artocarpus Integer): Sequences Of Its Subunits And Interactions With Human Serum O-Glycosylated Glycoproteins, Onn Haji Hashim Jan 2002

Galactose-Binding Lectin From The Seeds Of Champedak (Artocarpus Integer): Sequences Of Its Subunits And Interactions With Human Serum O-Glycosylated Glycoproteins, Onn Haji Hashim

Onn Haji Hashim

Our group has previously reported the isolation, partial characterisation, and application of a Galbeta1-3GalNAc- and IgA1-reactive lectin from the seeds of champedak (Artocarpus integer). In the present study, we have subjected the purified lectin to reverse-phase high performance liquid chromatography and sequenced its subunits. Determination of the N-terminal sequence of the first 47 residues of the large subunit demonstrated at least 95% homology to the N-terminal sequence of the alpha chains of a few other galactose-binding Artocarpus lectins, The two smaller subunits of the lectin, each comprised of 21 amino acid residues, demonstrated minor sequence variability. Their sequences were generally …