Tomato Pectin Methylesterase: Modeling, Fluorescence, and Inhibitor Interaction Studies - Comparison with the Bacterial (Erwinia chrysanthemi) Enzyme

Proteins: Structure, Function and Genetics

Volumn 53, Issue 4, 2003, Pages 830-839

  D'Avino, Rossana ^a   Camardella, Laura ^a   Christensen, Tove M I E ^b   Giovane, Alfonso ^c   Servillo, Luigi ^c  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^b DANISCO A S   (Denmark)

^c SECOND UNIVERSITY OF NAPLES   (Italy)

Author keywords

Fluorescence quenching; Molecular modeling; Pectin methylesterase; PME inhibitor; PME PMEI complex

Indexed keywords

BACTERIAL ENZYME; PECTINESTERASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CARROT; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME ISOLATION; ENZYME STRUCTURE; ERWINIA; FLUORESCENCE; KIWIFRUIT; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTON TRANSPORT; SPECIES DIFFERENCE; TOMATO;

AMINO ACID SEQUENCE; CARBOXYLIC ESTER HYDROLASES; CESIUM; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; DAUCUS CAROTA; ENZYME INHIBITORS; ERWINIA; IODIDES; ISOENZYMES; LYCOPERSICON ESCULENTUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, FLUORESCENCE;

ACTINIDIA CHINENSIS; BACTERIA (MICROORGANISMS); DAUCUS CAROTA; ERWINIA; ERWINIA CHRYSANTHEMI; LYCOPERSICON; LYCOPERSICON ESCULENTUM;

EID: 0344118134     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10487     Document Type: Article

References (29)

1. Willats WGT, Orfila C, Linberg G, Bucholt HC, van Alebeek GJWM, Voragen AGJ, Marcus SE, Christensen TMIE, Mikkelsen JD, Murray BS, Knox JP. Modulation of the degree and pattern of methyl-esterification of pectic homogalacturonan in plant cell walls. J Biol Chem 2001;276:19404-19413.
2. Limberg G, Korner R, Bucholt HC, Christensen TMIE, Roepstorff P, Mikkelsen JD. Analysis of different de-esterification mechanisms for pectin by enzymatic fingerprinting using endopectin lyase and endopolygalacturonase II from A. niger. Carbohydr Res 2000;27:293-307.
3. Micheli F. Pectin methylesterases: cell wall enzymes with important roles in plant physiology. Trends Plant Sci 2001;6:414-419.
4. Gaffe J, Tiznado ME, Handa AK. Characterization and functional expression of a ubiquitously expressed tomato pectin methylesterase. Plant Physiol 1997;14:1547-1556.
5. Micheli F, Sundberg B, Golberg R, Richard L. Radial distribution pattern of pectin methylesterases across the cambial region of hybrid aspen at activity and dormancy. Plant Physiol 2000;124:191-199.
6. Catoire L, Pierron M, Morvan C, Hervé du Penhoat C, Golberg R. Investigation of the action patterns of pectin methylesterase isoforms through kinetic analyses and NMR spectroscopy. Implications in cell wall expansion. J Biol Chem 1998;273:33150-33156.
7. Goldberg R, Pierron M, Bordenave M, Breton C, Morvan C, Hervé du Penhoat C. Control of mung bean pectinmethylesterase isoforms activities. Influence of pH and carboxyl group distribution along the pectic chain. J Biol Chem 2001;276:8841-8847.
8. Balestrieri C, Castaldo D, Giovane A, Quagliuolo L, Servillo L. A glycoprotein inhibitor of pectin methylesterase in kiwi fruit (Actinidia chinensis). Eur J Biochem 1990;193:183-187.
9. Giovane A, Balestrieri C, Quagliuolo L, Castaldo D, Servillo L. A glycoprotein inhibitor of pectin methylesterase in kiwi fruit. Purification by affinity chromatography and evidence of a ripening-related precursor. Eur J Biochem 1995;233:926-929.
10. Mattei B, Raiola A, Caprari C, Federici L, Bellincampi D, De Lorenzo G, Cervone F, Giovane A, Camardella L. Studies on plant inhibitors of pectin modifying enzymes: polygalacturonase-inhibiting protein (PGIP) and pectin methylesterase inhibitor (PMEI). In: Teeri TT, Svensson B, Gilbert HJ, Feizi T, editors. Carbohydrate bioengineering-interdisciplinary approaches. Bodmin, Cornwall, UK: MPG Books Ltd.; 2002. p 160-167.
11. Camardella L, Giovane A, Servillo L. Structure-function of a proteinaceous inhibitor of plant pectin methylesterase. In: Voragen AGJ, Schols HA, Visser RGF, editors. Advances in pectin and pectinase research. The Netherlands: Kluwer Academic Publishers; 2003. p 363-372.
12. Camardella L, Carratore V, Ciardiello MA, Servillo L, Balestrieri C, Giovane A. Kiwi protein inhibitor of pectin methylesterase. Amino acid sequence and structural importance of two disulfide bridges. Eur J Biochem 2000;267:4561-4565.
13. Jenkins J, Mayans O, Smith D, Worboys K, Pickersgill RW. Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site. J Mol Biol 2001;305:951-960.
14. Yoder MD, Keen NT, Jurnak F. New domain motif-the structure of pectate lyase C, a secreted plant virulence factor. Science 1993;260:1503-1507.
15. Markovič O, Stovičkova J, Jörnvall H. Modification of tomato and Aspergillus niger pectinesterase by diethyl pyrocarbonate. J Protein Chem 1996;15:127-130.
16. Johansson K, El-Amad M, Friemann R, Jörnvall H, Markovič O, Eklund H. Crystal structure of plant pectin methylesterase. FEBS Lett 2002;514:243-249.
17. Christensen TMIE, Brunstedt J, Bucholt HC, Mikkelsen JD. Demethylation pattern of pectin methyl esterase from Erwinia chrysanthemi. In: Pectins and pectinases 2001. Book of abstracts of an International Symposium, Rotterdam, The Netherlands, May 6-11, p. 83.
18. Giovane A, Quagliuolo L, Servillo L, Balestrieri C, Laratta B, Loiudice R, Castaldo D. Purification and characterization of three isozymes of pectin methylesterase from tomato fruit. J Food Biochem 1994;17:339-349.
19. Sander C, Schneider R. Database of homology-derived structures and the structural meaning of sequence alignment. Proteins 1991;9:56-68.
20. Rost B, Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 1994;19:55-77.
21. Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999;292:195-202.
22. Kelley LA, MacCallum RM, Sternberg MJE. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J Mol Biol 2000;299:499-520.
23. Greer J. Comparative modeling methods: application to the family of the mammalian serine protease. Proteins 1990;7:317-334.
24. Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial constraints. J Mol Biol 1993;234:779-815.
25. Yang JT. Calculation of protein conformation from circular dichroism. Methods Enzymol. 1986;130:208-269.
26. Lakowicz JR. Principles of fluorescence spectroscopy. New York-London: Plenum Press; 1983. p 279-284.
27. Markovič O, Jörnvall H. Pectinesterase. The primary structure of the tomato enzyme. Eur J Biochem 1986;158:455-462.
28. Markovič O, Jörnvall H. Disulfide bridges in tomato pectinesterase: variations from pectinesterases of other species; conservation of possible active segments. Protein Sci 1992;1:1288-1292.
29. Chen Y, Barkley MD. Toward understanding tryptophan fluorescence in proteins. Biochemistry 1998;37:9976-9982.