Cloning of a cDNA encoding a plasma membrane-associated, uronide binding phosphoprotein with physical properties similar to viral movement proteins.

Details

Serval ID
serval:BIB_7BF46369DBFB
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Cloning of a cDNA encoding a plasma membrane-associated, uronide binding phosphoprotein with physical properties similar to viral movement proteins.
Journal
Plant Cell
Author(s)
Reymond P., Kunz B., Paul-Pletzer K., Grimm R., Eckerskorn C., Farmer E.E.
ISSN
1040-4651 (Print)
ISSN-L
1040-4651
Publication state
Published
Issued date
1996
Volume
8
Number
12
Pages
2265-2276
Language
english
Abstract
Oligogalacturonides are structural and regulatory homopolymers from the extracellular pectic matrix of plants. In vitro micromolar concentrations of oligogalacturonates and polygalacturonates were shown previously to stimulate the phosphorylation of a small plasma membrane-associated protein in potato. Immunologically cross-reactive proteins were detected in plasma membrane-enriched fractions from all angiosperm subclasses in the Cronquist system. Polygalacturonate-enhanced phosphorylation of the protein was observed in four of the six dicotyledon subclasses but not in any of the five monocotyledon subclasses. A cDNA for the protein was cloned from potato. The deduced protein is extremely hydrophilic and has a proline-rich N terminus. The C-terminal half of the protein was predicted to be a coiled coil, suggesting that the protein interacts with other macromolecules. The recombinant protein was found to bind both simple and complex galacturonides. The behavior of the protein suggests several parallels with viral proteins involved in intercellular communication.
Keywords
Amino Acid Sequence, Base Sequence, Carrier Proteins/biosynthesis, Carrier Proteins/chemistry, Cell Membrane/metabolism, Cloning, Molecular, DNA, Complementary, Galactans/metabolism, Hexuronic Acids/metabolism, Molecular Sequence Data, Pectins/metabolism, Phosphoproteins/biosynthesis, Phosphoproteins/chemistry, Plant Proteins/biosynthesis, Plant Proteins/chemistry, Plant Viral Movement Proteins, Plants/metabolism, Recombinant Proteins/biosynthesis, Recombinant Proteins/chemistry, Sequence Homology, Amino Acid, Solanum tuberosum/metabolism, Viral Proteins/chemistry
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 20:05
Last modification date
20/08/2019 14:37
Usage data