Characterizing the Mechanisms of C. elegans PRMT1 Temperature Dependence

Authors

Arianna Towne, Utah State UniversityFollow

Files

Description

Over time, cellular enzymes evolve through amino acid mutations which allow them to remain functional at temperatures specific to the host organism. This activity may be partially or completely lost when enzymes are removed from their optimal temperature range, as is observed for the C. elegans protein arginine methyltransferase 1 (cPRMT1). This construct demonstrates maximum enzymatic activity at the C. elegans optimum of 20°C, but no activity at 37°C where activity for mammalian PRMT1 variants is observed. Given dysregulation of PRMT1 has been linked to various disease states, we are interested in exploiting the biophysical mechanisms of cPRMT1 temperature dependence to improve our understanding of catalysis and regulatory means of this enzyme family.

Publication Date

12-9-2021

City

Logan, UT

Keywords

temperature dependence, protein modification, post-production tags, protein regulation

Disciplines

Biochemistry

Recommended Citation

Towne, Arianna, "Characterizing the Mechanisms of C. elegans PRMT1 Temperature Dependence" (2021). Fall Student Research Symposium 2021. 16.
https://digitalcommons.usu.edu/fsrs2021/16