Drosera Capensis’ Protein Analysis – Morning Sign Out at UCI

Written by Amal Gaiz El Ali

Drosera capensis is a carnivorous plant which has a variety of proteins. There are a large number of proteins that have yet to still be sequenced and discovered. One such protein found in the Drosera plant is the chitinase protein. Chitinase is an enzyme that degrades chitin, but it plays a role in pathogen control, wound treatment, and metabolism [3]. The chitinase protein has many different family groups, classified by the ways in which the protein can fold [2]. The different folding of each protein allows for a different form, and thus although the protein is a form of chitinase, it functions differently.

Oftentimes, if a protein such as chitinase does not fold properly, it will fail to perform its corresponding function. Lacking chitinase protein in a carnivorous plant can be detrimental because the plant relies heavily on the enzyme to break down the chitin it produces. If the enzyme is missing in the plant, the chitin will build up excessively and can greatly harm the plant.

Scientists at the University of California, Irvine have been attempting to sequence the various chitinase proteins. Sequencing the chitinase enzymes will allow scientists to classify them and reveal their function. Once the function of a chitinase protein is discovered, scientists can utilize this knowledge to help classify other proteins and determine their functions. If a protein is classified but does not perform its designated function, researchers will then look at the binding sites to discover if the protein may have been misfolded.

Dr. Rachel Martin at the University of California, Irvine, utilizes genomic sequencing to discover new proteins found in the carnivorous plant, Drosera capensis. By utilizing bioinformatics the protein structure can be analyzed in depth to figure out the binding sites. Bioinformatics is the process of collecting and analyzing complex biological data, such as protein sequences [1]. By doing so, scientists have an idea of what the protein should be like and can conduct further research to prevent the aggregation of incorrect proteins. Understanding the various characteristics of aggregated proteins can lead to a better understanding of diseases that this aggregation can cause.

A second-year graduate student in the Martin Lab, Vy Duong, focuses primarily on the computational aspect of determining the protein structure. When asked about what her ultimate goal in her research at the Martin Lab is, Duong simply responded, “To learn.” Duong explained that since very little is known about the various proteins in the Drosera capensis plant, we cannot fully understand the importance of the protein, but by researching and analyzing the sequence, the structure and the function in the plant, we can use this knowledge to advance our own lives.

The Martin Lab predominantly focuses on proving predicted structures. Dr. Martin sequences the proteins, and using this sequence, predicts the structure and function through an online source known as Rosetta. Researchers in the lab then use plasmids and other methods to prove that the predicted structure and function are the actual intended behavior and form of the protein.
Observing the structure and characteristics of proteins such as chitinase allows for further understanding of how folding incorrectly can overall change the function of the protein not only in Drosera capensis, but also in human beings.

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