Characterization of C-Gmp Dependent Kinases Within the Circadian Molecular Clockworks: Structural, Phylogenetic, and Functional Analyses
Pace, Laura A.
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https://hdl.handle.net/2142/82517
Description
Title
Characterization of C-Gmp Dependent Kinases Within the Circadian Molecular Clockworks: Structural, Phylogenetic, and Functional Analyses
Author(s)
Pace, Laura A.
Issue Date
2007
Doctoral Committee Chair(s)
Gillette, Martha U.
Department of Study
Neuroscience
Discipline
Neuroscience
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Neuroscience
Language
eng
Abstract
cGKI and cGKII are paralogous serine/threonine protein kinases. In an effort to determine the mechanism by which the circadian molecular clockworks differentially regulates the activity of these kinases a comparative biology approach was employed. This work included phylogenetic and 3-dimensional homology based structural analysis of the AGC Group which includes the cGK family. This work identifies new members of the cGK family across the eukaryotic tree and proposes a new definition for the cGK family that is based on phylogenetic and structural analysis of the protein rather than the specific cyclic nucleotide activator. Phylogenetic analysis of the entire cGK family demonstrates that the gene duplication that lead to the Prkg1 and Prkg2 genes found within extant vertebrate metazoans actually occurred before the Arthropoda split from the Chordata lineage and that the Prkg2 gene is the ancestral gene of the cGK family. Homology based structural models of the functional domains of the cGK family indicate impressive conservation within the cyclic nucleotide binding domains and within the catalytic loop and activation segment as well as the substrate binding cleft. We propose that cGK family members vary their intracellular location and interaction partners via differences in their amine-terminus in an effort to target specific substrates rather than varying their canonical substrate recognition sequence.
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