title: Polygalacturonase-inhibiting protein is a structural component of plant cell wall.
abstract: It is generally believed that plants "evolved a strategy of defending themselves from a phytopathogen attack" during evolution. This metaphor is used frequently, but it does not facilitate understanding of the mechanisms providing plant resistance to the invasion of foreign organisms and to other unfavorable external factors, as well as the role of these mechanisms in plant growth and development. Information on processes involving one of the plant resistance factors--polygalacturonase-inhibiting protein (PGIP)--is considered in this review. The data presented here indicate that PGIP, being an extracellular leucine-rich repeat-containing protein, performs important functions in the structure of plant cell wall. Amino acid residues participating in PGIP binding to homogalacturonan in the cell wall have been determined. The degree of methylation and the mode of distribution of homogalacturonan methyl groups are responsible for the formation of a complex structure, which perhaps determines the specificity of PGIP binding to pectin. PGIP is apparently one of the components of plant cell wall determining some of its mechanical properties; it is involved in biochemical processes related to growth, expansion, and maceration, and it influences plant morphology. Polygalacturonase (PG) is present within practically all plant tissues, but the manifestation of its activity varies significantly depending on physiological conditions in the tissue. Apparently, the regulation of PG functioning in apoplast significantly affects the development of processes associated with the modification of the structure of plant cell wall. PGIP can regulate PG activity through binding to homogalacturonan. The genetically determined structure of PGIP in plants determines the mode of its interaction with an invader and perhaps is one of the factors responsible for the set of pathogens causing diseases in a given plant species.
authors.affiliation: Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia. protsenko@inbi.ras.ru
authors.forename: M A
authors.initials: MA
authors.lastname: Protsenko
authors.forename: N L
authors.initials: NL
authors.lastname: Buza
authors.forename: A A
authors.initials: AA
authors.lastname: Krinitsyna
authors.forename: E A
authors.initials: EA
authors.lastname: Bulantseva
authors.forename: N P
authors.initials: NP
authors.lastname: Korableva
mesh_terms: D002473:Cell Wall / Q000378:metabolism*; D000090263:Leucine-Rich Repeat Proteins; D008954:Models, Biological; D010935:Plant Diseases; D010940:Plant Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D011096:Polygalacturonase / Q000037:antagonists & inhibitors; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism
chemical_list: D000090263:Leucine-Rich Repeat Proteins; C081479:PGIP protein, plant; D010940:Plant Proteins; D011506:Proteins; D011096:Polygalacturonase