Reduction in Pectin Methylesterase Activity Modifies Tissue Integrity and Cation Levels in Ripening Tomato (Lycopersicon esculentum Mill.) Fruits

Pectin methylesterase (PME, EC 3.1.1.11) is an ubiquitous enzyme in the plant kingdom; however, its role in plant growth and development is not yet understood. Using transgenic tomato (Lycopersicon esculentum Mill.) fruits that show more than 10-fold reduction in PME activity because of expression of an antisense PME gene, we have investigated the role of PME in tomato fruit ripening. Our results show that reduced PME activity causes an almost complete loss of tissue integrity during fruit senescence but shows little effect on fruit firmness during ripening. Low PME activity in the transgenic fruit pericarp modified both accumulation and partitioning of cations between soluble and bound forms and selectively impaired accumulation of Mg2+ over other major cations. Decreased PME activity was associated with a 30 to 70% decrease in bound Ca2+ and Mg2+ in transgenic pericarp. Levels of soluble Ca2+ increase 10 to 60%, whereas levels of soluble Mg2+ and Na+ are reduced by 20 to 60% in transgenic pericarp. Changes in cation levels associated with lowered PME activity do not affect the rate of respiration or membrane integrity of fruit during ripening. Overall, these results suggest that PME plays a role in determining tissue integrity during fruit senescence, perhaps by regulating cation binding to the cell wall.

[1]  D. Tieman,et al.  Pectin Methylesterase Isoforms in Tomato (Lycopersicon esculentum) Tissues (Effects of Expression of a Pectin Methylesterase Antisense Gene) , 1994, Plant physiology.

[2]  J. Labavitch,et al.  Cell Wall Metabolism in Ripening Fruit (VI. Effect of the Antisense Polygalacturonase Gene on Cell Wall Changes Accompanying Ripening in Transgenic Tomatoes) , 1993, Plant physiology.

[3]  J. Ray,et al.  Antisense inhibition of pectin esterase gene expression in transgenic tomatoes , 1993 .

[4]  N. Carpita,et al.  Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. , 1993, The Plant journal : for cell and molecular biology.

[5]  L. Staehelin,et al.  Domain-specific and cell type-specific localization of two types of cell wall matrix polysaccharides in the clover root tip , 1992, The Journal of cell biology.

[6]  D. Tieman,et al.  An Antisense Pectin Methylesterase Gene Alters Pectin Chemistry and Soluble Solids in Tomato Fruit. , 1992, The Plant cell.

[7]  B. Vian,et al.  Immunocytochemical study of the deesterification patterns during cell wall autolysis in the ripening of cherry tomato , 1992 .

[8]  G. Tucker,et al.  Fruit Quality Characteristics of Transgenic Tomato Fruit with Altered Polygalacturonase Activity , 1991 .

[9]  A. Bennett,et al.  ROLE OF CELL WALL HYDROLASES IN FRUIT RIPENING , 1991 .

[10]  Alan G. Darvill,et al.  The Pectic Polysaccharides of Primary Cell Walls , 1990 .

[11]  J. Letesson,et al.  Monoclonal Antibodies against Pectin: Recognition of a Conformation Induced by Calcium. , 1989, Plant physiology.

[12]  D. Nevins,et al.  Tomato fruit cell wall : I. Use of purified tomato polygalacturonase and pectinmethylesterase to identify developmental changes in pectins. , 1989, Plant physiology.

[13]  J. Varner,et al.  New ways to look at the architecture of plant cell walls : localization of polygalacturonate blocks in plant tissues. , 1989, Plant physiology.

[14]  M. Saltveit Effect of alcohols and their interaction with ethylene on the ripening of epidermal pericarp discs of tomato fruit. , 1989, Plant physiology.

[15]  M. S. Biggs,et al.  Temporal regulation of polygalacturonase gene expression in fruits of normal, mutant, and heterozygous tomato genotypes. , 1989, Plant physiology.

[16]  A. Reddy,et al.  Calcium and fruit softening: physiology and biochemistry , 1988 .

[17]  Joseph E. Varner,et al.  Cell Wall Proteins , 1988 .

[18]  G. Tucker,et al.  Differential effects of pectolytic enzymes on tomato polyuronides in vivo and in vitro , 1987 .

[19]  H. Marschner Mineral Nutrition of Higher Plants , 1988 .

[20]  D. Northcote Control of Pectin Synthesis and Deposition during Plant Cell Wall Growth , 1986 .

[21]  D. Huber,et al.  Comparative Analysis of Pectins from Pericarp and Locular Gel in Developing Tomato Fruit , 1986 .

[22]  Stephen C. Fry,et al.  Cross-Linking of Matrix Polymers in the Growing Cell Walls of Angiosperms , 1986 .

[23]  P. Albersheim,et al.  Structure of the backbone of rhamnogalacturonan i a pectic polysaccharide in the primary cell walls of plants , 1985 .

[24]  R. Wayne,et al.  CALCIUM AND PLANT DEVELOPMENT , 1985 .

[25]  I. Ferguson Calcium in plant senescence and fruit ripening , 1984 .

[26]  Maurice Demarty,et al.  Calcium and the cell wall , 1984 .

[27]  M. Jarvis Structure and properties of pectin gels in plant cell walls , 1984 .

[28]  R. Buescher,et al.  ROLE OF CALCIUM AND CHELATING AGENTS IN REGULATING THE DEGRADATION OF TOMATO FRUIT TISSUE BY POLYGALACTURONASE , 1982 .

[29]  J. Roberts,et al.  Cell Biology of Abscission , 1982 .

[30]  E. Morris,et al.  Conformations and interactions of pectins. II. Influences of residue sequence on chain association in calcium pectate gels. , 1982, Journal of molecular biology.

[31]  E. Morris,et al.  Conformations and interactions of pectins. I. Polymorphism between gel and solid states of calcium polygalacturonate. , 1982, Journal of molecular biology.

[32]  R. Pressey,et al.  SOLUBILIZATION OF CELL WALLS BY TOMATO POLYGALACTURONASES: EFFECTS OF PECTINESTERASES , 1982 .

[33]  S. Arnott,et al.  Conformations and interactions of pectins. II. Models for junction zones in pectinic acid and calcium pectate gels. , 1981, Journal of molecular biology.

[34]  B. Poovaiah,et al.  Association between Elemental Content and Fruit Ripening in rin and Normal Tomatoes. , 1978, Plant physiology.

[35]  E. Morris,et al.  Biological interactions between polysaccharides and divalent cations: The egg‐box model , 1973 .

[36]  H. Lineweaver,et al.  Pectic Enzymes , 1955, Nature.