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Functional and structural characterization of the catalytic domain of the starch synthase III from Arabidopsis thaliana.
Proteins. 2008 Jan 01; 70(1):31-40.P

Abstract

Glycogen and starch are the major energy storage compounds in most living organisms. The metabolic pathways leading to their synthesis involve the action of several enzymes, among which glycogen synthase (GS) or starch synthase (SS) catalyze the elongation of the alpha-1,4-glucan backbone. At least five SS isoforms were described in Arabidopsis thaliana; it has been reported that the isoform III (SSIII) has a regulatory function on the synthesis of transient plant starch. The catalytic C-terminal domain of A. thaliana SSIII (SSIII-CD) was cloned and expressed. SSIII-CD fully complements the production of glycogen by an Agrobacterium tumefaciens glycogen synthase null mutant, suggesting that this truncated isoform restores in vivo the novo synthesis of bacterial glycogen. In vitro studies revealed that recombinant SSIII-CD uses with more efficiency rabbit muscle glycogen than amylopectin as primer and display a high apparent affinity for ADP-Glc. Fold class assignment methods followed by homology modeling predict a high global similarity to A. tumefaciens GS showing a fully conservation of the ADP-binding residues. On the other hand, this comparison revealed important divergences of the polysaccharide binding domain between AtGS and SSIII-CD.

Authors+Show Affiliations

Busi MV
IIB-INTECH, CONICET-UNSAM, Camino Circunvalación km 6, 7130, Chascomús, Buenos Aires, Argentina.
Palopoli N
No affiliation info available
Valdez HA
No affiliation info available
Fornasari MS
No affiliation info available
Wayllace NZ
No affiliation info available
Gomez-Casati DF
No affiliation info available
Parisi G
No affiliation info available
Ugalde RA
No affiliation info available

MeSH

ArabidopsisArabidopsis ProteinsBase SequenceCatalytic DomainCloning, MolecularComputational BiologyDNA PrimersElectrophoresis, Polyacrylamide GelGlucosyltransferasesModels, MolecularProtein ConformationSubstrate Specificity

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17623838

Citation

Busi, Maria V., et al. "Functional and Structural Characterization of the Catalytic Domain of the Starch Synthase III From Arabidopsis Thaliana." Proteins, vol. 70, no. 1, 2008, pp. 31-40.
Busi MV, Palopoli N, Valdez HA, et al. Functional and structural characterization of the catalytic domain of the starch synthase III from Arabidopsis thaliana. Proteins. 2008;70(1):31-40.
Busi, M. V., Palopoli, N., Valdez, H. A., Fornasari, M. S., Wayllace, N. Z., Gomez-Casati, D. F., Parisi, G., & Ugalde, R. A. (2008). Functional and structural characterization of the catalytic domain of the starch synthase III from Arabidopsis thaliana. Proteins, 70(1), 31-40.
Busi MV, et al. Functional and Structural Characterization of the Catalytic Domain of the Starch Synthase III From Arabidopsis Thaliana. Proteins. 2008 Jan 1;70(1):31-40. PubMed PMID: 17623838.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Functional and structural characterization of the catalytic domain of the starch synthase III from Arabidopsis thaliana. AU - Busi,Maria V, AU - Palopoli,Nicolas, AU - Valdez,Hugo A, AU - Fornasari,Maria S, AU - Wayllace,Nahuel Z, AU - Gomez-Casati,Diego F, AU - Parisi,Gustavo, AU - Ugalde,Rodolfo A, PY - 2007/7/12/pubmed PY - 2008/1/17/medline PY - 2007/7/12/entrez SP - 31 EP - 40 JF - Proteins JO - Proteins VL - 70 IS - 1 N2 - Glycogen and starch are the major energy storage compounds in most living organisms. The metabolic pathways leading to their synthesis involve the action of several enzymes, among which glycogen synthase (GS) or starch synthase (SS) catalyze the elongation of the alpha-1,4-glucan backbone. At least five SS isoforms were described in Arabidopsis thaliana; it has been reported that the isoform III (SSIII) has a regulatory function on the synthesis of transient plant starch. The catalytic C-terminal domain of A. thaliana SSIII (SSIII-CD) was cloned and expressed. SSIII-CD fully complements the production of glycogen by an Agrobacterium tumefaciens glycogen synthase null mutant, suggesting that this truncated isoform restores in vivo the novo synthesis of bacterial glycogen. In vitro studies revealed that recombinant SSIII-CD uses with more efficiency rabbit muscle glycogen than amylopectin as primer and display a high apparent affinity for ADP-Glc. Fold class assignment methods followed by homology modeling predict a high global similarity to A. tumefaciens GS showing a fully conservation of the ADP-binding residues. On the other hand, this comparison revealed important divergences of the polysaccharide binding domain between AtGS and SSIII-CD. SN - 1097-0134 UR - https://www.unboundmedicine.com/medline/citation/17623838/Functional_and_structural_characterization_of_the_catalytic_domain_of_the_starch_synthase_III_from_Arabidopsis_thaliana_ L2 - https://doi.org/10.1002/prot.21469 DB - PRIME DP - Unbound Medicine ER -