Authors:

Manasa Addagarla

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About Paper:

Site-Directed Mutagenesis Glycerol kinase (GK) is a crucial enzyme in the halophilic archaeon Haloferax volcanii, playing a pivotal role in glycerol metabolism and stress protection. Post-translational modifications, such as lysine acetylation, can modulate the activity and function of enzymes, thereby influencing cellular processes. This study aims to investigate the impact of lysine acetylation on the function of GK from Haloferax volcanii through site-directed mutagenesis. The lysine residue at position 153 (K153) of the GK sequence was targeted for mutagenesis producing two mutant variants. K153Q mimics the deacetylated state by substituting lysine with arginine, and K153Q, mimics the acetylated state by substituting lysine with glutamine. The findings from this study will provide insights into the role of lysine acetylation in regulating the activity and function of GK in Haloferax volcanii. Understanding the impact of post-translational modifications on this crucial enzyme could shed light on the adaptive mechanisms employed by this halophilic archaeon to thrive in extreme environments. 470

Source:

University of Florida / 2024

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Co-authors:

Manasa Addagarla