Search research reports:
Chloroplast-Localized Co- and Post-Translational Processing Enzymes: Essential Determinants of Protein Maturation
Department of Horticulture
Co- and post-translational protein processing is often essential through influences on protein folding, stability, turnover, and activity. Additionally, it changes protein identity from that which can be deduced from DNA translation in unpredictable ways. Within the limited proteome of the chloroplast, a plethora of protein processing occurs, which, while recently physically characterized through newly developed techniques in mass spectroscopy polypeptide fingerprinting, have yet to be exploited through biochemical characterization of the associated enzymes, perhaps due to the inherent challenges therein.
The following studies capitalize on existing and previous accomplishments from the author's laboratory, widely recognized for discoveries in chloroplast-localized co- and post-translational protein processing. Application of these skills and abilities to the currently unknown areas of co- and post-translational processing enzymes in the chloroplast will provide information which allows prediction of protein processing and maturation in the chloroplast of all plants.
2011 Project Description
Experiments were conducted to evaluate the methylation status of calmodulin in lymphoblastoid cells from patience's with 2p21 gene deletion syndrome. Additional experiments were conducted to evaluate the methyltransferase activity of a SET 7/9 mutant enzyme with an unnatural amino acid substitution in place of an active-site tyrosine residue. Two undergraduate students were mentored on research projects relative to these experiments.
Calmodulin methyltransferase (Cam KMT) was identified in insects, rats, mice, and plants. An alternatively spiced short isoform of Cam KMT was identified in humans and characterized.
Whitney, S. M., R. L. Houtz, et al. (2011). Advancing our understanding and capacity to engineer nature's CO2-sequestering enzyme, Rubisco. Plant Physiology 155(1):27-35.