91¾«¼ò°æ

Madushi Raththagala

Associate Professor of Chemistry

Office: CIS 210E
Phone: 518-580-8193
Email: mraththa@skidmore.edu

EDUCATION

• B.Sc. (Honors) Biochemistry and Molecular Biology 2002, University of Colombo, Sri Lanka

• Ph.D. Chemistry 2008, Michigan State University

• Postdoctoral Researcher, Johns Hopkins University, 2010-2012

• Postdoctoral Researcher, University of Kentucky, 2012-2017  

At 91¾«¼ò°æ since 2017

 

RESEARCH

Starch is the primary carbon storage form of most plants, a source of calories in the human diet, and an important raw material for various industrial applications. Transitory starch is synthesized in the chloroplast stroma during the daytime and degraded at night to generate energy for cellular metabolism, growth, and storage. Transitory starch metabolism is closely related to the entire biology of the plant as it serves as the primary carbon source for various metabolic processes. Despite the significant amounts of genetics, biochemical, physiological, and molecular level information available on starch synthesis and degradation, there are several unresolved areas in transitory starch metabolism, including: 1) Structure of the starch granule is not well defined; 2) Role of starch phosphorylation is not entirely understood; and 3) Regulation of starch degradation is not clearly understood. Understanding starch degradation at the molecular level not only increases our understanding of plant growth and development but also allows us to manipulate crops to better serve current global needs.
 
Our NSF-funded research program at 91¾«¼ò°æ is focused on how reversible starch phosphorylation regulates transitory and storage starch metabolism in photosynthetic organisms. Carbohydrate phosphorylation is emerging as a critical signaling event that initiates and regulates plant starch metabolism and animal glycogen metabolism. We are interested in understanding how glucan phosphatases and dikinases, central enzyme families in reversible starch phosphorylation, integrate signaling events to initiate, coordinate, and regulate transitory and storage starch metabolism. 
 
In the lab, we utilize tools from biochemistry, molecular biology, and biophysical methods to investigate how these enzyme families regulate starch metabolism and collaborate with experts in the field for X-ray crystallography studies. Our research represents a robust combination of advancing foundational research, improving undergraduate education, and positively impacting future agricultural and industrial applications.

COURSES

• CH 125 - Principles of Chemistry
• CH 341 - Biochemistry: Macromolecular Structure and Function with Lab
• CH342 - Intermediary Metabolism
• CH343 - Experimental Biochemistry Lab
• CH351 - Structural Biochemistry (Chemistry Elective)
• ID222- Minoritized Identities in Science (Bridge Course)

PUBLICATIONS 

(* denotes the corresponding author, underline denotes 91¾«¼ò°æ undergraduates)

1. Eliana Wolpaw, Marissa Frenett, Sloane Zwanger, Claudia Mak, and Madushi Raththagala*. (2023), Concanavalin-based In-vitro Sedimentation Assay for Characterizing     glucan Phosphatase-Starch Interaction, Journal of Visual Experimentation, 190, 10.3791/64700
2. Marissa L. Frenett, Kenyon Weis, Molly J. Cole, Juan Carlos Cruz, Alyssa Ramsay, Jiayue Huang, Matthew S. Gentry, Craig W. Vander Kooi, Madushi Raththagala* (2022), Differential Activity of Glucan Phosphatase Starch EXcess4 Orthologs from Agronomic Crops, Biocatalysis and Agricultural Biotechnology, 45, 102479
    
3. Mak, C. A., Weis, K., Henao, T., Kuchtova, A., Chen, T., Sharma, S., Meekins, D. A., Thalmann, M., Vander Kooi, C. W., and Raththagala, M.* (2021) Cooperative Kinetics of the Glucan Phosphatase Starch Excess4. Biochemistry 60, 2425-2435
    
4. Wilkens, C., Auger, K. D., Anderson, N. T., Meekins, D. A., Raththagala, M., Abou Hachem, M., Payne, C. M., Gentry, M. S., and Svensson, B. (2016) Plant alpha-glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose. FEBS letters 590, 118-128
    
5. Romá-Mateo, C., Raththagala, M., Gentry, M. S., and Sanz, P. (2016) Assessing the Biological Activity of the Glucan Phosphatase Laforin. Methods in molecular biology (Clifton, N.J.) 1447, 107-119
    
6. Raththagala, M., Brewer, M. K., Parker, M. W., Sherwood, A. R., Wong, B. K., Hsu, S., Bridges, T. M., Paasch, B. C., Hellman, L. M., Husodo, S., Meekins, D. A., Taylor, A. O., Turner, B. D., Auger, K. D., Dukhande, V. V., Chakravarthy, S., Sanz, P., Woods, V. L., Jr., Li, S., Vander Kooi, C. W., and Gentry, M. S. (2015) Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease. Molecular cell 57, 261-272
    
7. Meekins, D. A., Raththagala, M., Auger, K. D., Turner, B. D., Santelia, D., Kötting, O., Gentry, M. S., and Vander Kooi, C. W. (2015) Mechanistic Insights into Glucan Phosphatase Activity against Polyglucan Substrates. The Journal of biological chemistry 290, 23361-23370
    
8. Clark, N. J., Raththagala, M., Wright, N. T., Buenger, E. A., Schildbach, J. F., Krueger, S., and Curtis, J. E. (2014) Structures of TraI in solution. Journal of molecular modeling 20, 2308
    
9. Meekins, D. A., Raththagala, M., Husodo, S., White, C. J., Guo, H. F., Kotting, O., Vander Kooi, C. W., and Gentry, M. S. (2014) Phosphoglucan-bound structure of starch phosphatase Starch Excess4 reveals the mechanism for C6 specificity. Proceedings of the National Academy of Sciences of the United States of America 111, 7272-7277
    
10. Sánchez-Martín, P., Raththagala, M., Bridges, T. M., Husodo, S., Gentry, M. S., Sanz, P., and Romá-Mateo, C. (2013) Dimerization of the glucan phosphatase laforin requires the participation of cysteine 329. PloS one 8, e69523
11. Wright, N. T., Raththagala, M., Hemmis, C. W., Edwards, S., Curtis, J. E., Krueger, S., and Schildbach, J. F. (2012) Solution structure and small angle scattering analysis of TraI (381-569). Proteins 80, 2250-2261
12. Raththagala, M., Karunarathne, W., Kryziniak, M., McCracken, J., and Spence, D. M. (2010) Hydroxyurea stimulates the release of ATP from rabbit erythrocytes through an increase in calcium and nitric oxide production. European journal of pharmacology 645, 32-38
13. Tolan, N. V., Genes, L. I., Subasinghe, W., Raththagala, M., and Spence, D. M. (2009) Personalized metabolic assessment of erythrocytes using microfluidic delivery to an array of luminescent wells. Analytical chemistry 81, 3102-3108
14. Carroll, J., Raththagala, M., Subasinghe, W., Baguzis, S., D'Amico Oblak, T., Root, P., and Spence, D. (2006) An altered oxidant defense system in red blood cells affects their ability to release nitric oxide-stimulating ATP. Molecular bioSystems 2, 305-311
15. Raththagala, M., Root, P. D., and Spence, D. M. (2006) Dynamic monitoring of glutathione in erythrocytes, without a separation step, in the presence of an oxidant insult. Analytical chemistry 78, 8556-8560.(2022), Differential Activity of Glucan Phosphatase Starch EXcess4 Orthologs from Agronomic Crops, Biocatalysis and Agricultural Biotechnology, 45, 102479
     

PROFESSIONAL MEMBERSHIPS

• American Chemical Society (ACS)
• American Society of Biochemistry and Molecular Biology (ASBMB)
• American Association for the Advancement of Science (AAAS)