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Characterization of Caenorhabditis Elegans Mechanosensory Protein-6 (Mec-6)

Characterization of Caenorhabditis Elegans Mechanosensory Protein-6 (Mec-6)


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Identified in Caenorhabditis elegans, the mec-6 complementary DNA (cDNA) encodes a polypeptide of 377 amino acids that is 25% identical and 45% similar over a stretch of 250 amino acids at its carboxy terminus to vertebrate paraoxonase (PON) family of proteins. The PON family consists of three family members (PON1, PON2 and PON3) that are share structural properties and enzymatic activities. PON proteins are calcium (Ca2+) dependent cysteine directed esterases with a broad range of substrate specificities including aryl-esters, lactones and organophosphates. Recently, in addition to their role in hydrolyzing toxic organophosphate compounds, PONs have been shown to play an important role in lipid metabolism and a protective role against cardiovascular disease and atherosclerosis. The conservation of homology and the high similarity in structural characteristics with the mammalian PONs led me to investigate the functional similarities of the C. elegans PON homolog MEC-6. I hypothesized that MEC-6 possesses equivalent hydrolase activities found in human (and animal) PON proteins. In this work, I have compared functional activities of affinity purified recombinant expressed MEC-6 protein (rMEC-6) with those of recombinant human PON-1 protein (rhPON1). My studies revealed that rMEC-6 catalyzes the hydrolysis of two known substrates (phenyl acetate and dihydrocoumarin) of the PON family, indicating that MEC-6 has the ability to function both as an arylesterase and a lactonase, respectively. In addition, these hydrolytic activities of rMEC-6 were sensitive to the addition of a metal chelator such as ethylene diamine tetra acetic acid (EDTA) suggesting rMEC-6 activity, like its mammalian PON homologs, is Ca2+ dependent. Inhibition studies using sulfhydryl blocking agent, para-hydroxymercuribenzoate (PHMB), revealed that a free sulfhydryl group is likely to be responsible for enzymatic activity of rMEC-6. The PON proteins have three highly conserved cysteine (C) residues (C41, C284 and C352) which are thought to be important for their esterase and anti-oxidative functions. MEC-6 has a total of five cysteine residues, including the two highly conserved structural cysteines (numbered C48 and C369 in MEC-6). My approach was to examine whether changes in rMEC-6 protein, through engineered cysteine substitutions, could modulate the enzymatic abilities of the recombinant protein. To determine the role of the cysteine residues in rMEC-6 in its enzymatic functions, I performed site-directed mutagenesis of each cysteine residue replacing it with an alanine residue (A). I then tested the effects of these mutations in the rMEC-6 protein's ability to act as an arylesterase and lactonase. In the rMEC-6 protein, replacement of C25, C48 and C170 with an alanine residue resulted in a complete loss of rMEC-6 arylesterase and lactonase activities; whereas, replacement of either C151 or C369 were without effect. In summary, these studies reveal a novel role for MEC-6 in vitro . Similar to its mammalian PON family homologs, MEC-6 acts as a Ca 2+ dependent esterase. Inhibitor studies revealed that a free sulfhydryl group is responsible for the enzymatic activity of rMEC-6. Site-directed mutagenesis of the cysteine residues of recombinantly expressed rMEC-6 revealed that the replacement of C25, C48, or C151 with an alanine residue results in significant loss of wild type rMEC-6 functions in the enzymatic activities. Although the function of MEC-6's enzymatic activities in C. elegans has yet to be elucidated, this study has revealed specific analogous functional activities to its mammalian PON homologs. Given the importance of the role of vertebrate PONs, it...


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Product Details
  • ISBN-13: 9781243998170
  • Publisher: Proquest, Umi Dissertation Publishing
  • Publisher Imprint: Proquest, Umi Dissertation Publishing
  • Height: 246 mm
  • Weight: 213 gr
  • ISBN-10: 1243998172
  • Publisher Date: 01 Sep 2011
  • Binding: Paperback
  • Spine Width: 6 mm
  • Width: 189 mm


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Characterization of Caenorhabditis Elegans Mechanosensory Protein-6 (Mec-6)
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Characterization of Caenorhabditis Elegans Mechanosensory Protein-6 (Mec-6)
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