The Systemin Receptor SR160 from Lycopersicon peruvianum is a Member of the LRR Receptor Kinase Family

The isolation to homogeneity of the 160-kDa systemin cell-surface receptor (SR160) from plasma membranes of suspension cultured cells of Lycopersicon peruvianum is reported. The purification procedure resulted in recovery of 13 µg of pure receptor protein, representing an 8,200-fold purification. Ge...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 99; no. 14; pp. 9585 - 9590
Main Authors Scheer, Justin M., Ryan, Clarence A.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 09.07.2002
National Acad Sciences
SeriesFrom the Cover
Subjects
Amino Acid Sequence
Amino acids
Base Sequence
Biological Sciences
Cells
Chemical suspensions
Complementary DNA
Cultured cells
DNA
DNA, Plant - genetics
Enzymes
Flowers & plants
Gels
Genes, Plant
Lycopersicon esculentum - genetics
Lycopersicon esculentum - metabolism
Molecular Sequence Data
Peptides
Peptides - metabolism
Plant cells
Plant Proteins - genetics
Plant Proteins - metabolism
Protein Kinases - genetics
Protein Kinases - metabolism
Proteins - genetics
Proteins - metabolism
Radioactive decay
Receptors
Resins
Sequence Homology, Amino Acid
Tomatoes
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Summary:The isolation to homogeneity of the 160-kDa systemin cell-surface receptor (SR160) from plasma membranes of suspension cultured cells of Lycopersicon peruvianum is reported. The purification procedure resulted in recovery of 13 µg of pure receptor protein, representing an 8,200-fold purification. Gel blot analyses using SR160-specific antibodies confirmed that a cross-reacting protein in the membranes of suspension-cultured cells comigrates with both the native and a deglycosylated form of the radiolabeled receptor. Internal amino acid sequences of the purified protein facilitated the isolation of a cDNA clone encoding the 160-kDa receptor. The identity of the encoded protein as SR160 was further confirmed by a comparison of its sequence with a mass spectral fingerprint of the SR160 protein. The deduced amino acid sequence of SR160 revealed that it is a member of the leucine-rich repeat (LRR) receptor kinase family, closely related to the brassinolide receptor kinase, BRI1.
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Contributed by Clarence A. Ryan, Jr.
To whom reprint requests should be addressed. E-mail: cabudryan@hotmail.com.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.132266499