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Identification and characterization of Caenorhabditis elegans genes encoding fatty acid beta-oxidation proteins using Saccharomyces cerevisiae as surrogate system

Identification and characterization of Caenorhabditis elegans genes encoding fatty acid beta-oxidation proteins using Saccharomyces cerevisiae as surrogate system

Aner Gurvitz (ORCID: )
  • Grant DOI 10.55776/P14837
  • Funding program Principal Investigator Projects
  • Status ended
  • Start February 1, 2002
  • End December 31, 2002
  • Funding amount € 18,960

Disciplines

Biology (100%)

Keywords

    PEROXISOMES, SACCHAROMYCES CEREVISIAE, BETA-OXIDATION, PTS1, CAENORHABDITIS ELEGANS, PEX-5

Abstract

Inherited human peroxisomal diseases such as Zellweger syndrome often lead to problems in neuronal development and to neurodegeneration. In addition to containing enzymes catalyzing reactions involving molecular oxygen and for metabolising hydrogen peroxide, peroxisomes are also involved in degrading fatty acids. An established model organism for studies on neural development and maintenance is represented by the nematode Caenorhabditis elegans. The neural network in C. elegans has been thoroughly studied, and its genome has now been sequenced. However, little is known about peroxisomes or fatty acid degradation in this organism. Hence, as a first step in assessing whether nematodes could serve as an appropriate model system for studying the potential role of peroxisomes and peroxisomal functions in neurodegeneration, more information must be obtained about the nematode peroxisomal compartment as well as the identity of the biochemical processes contained therein. To identify nematode ?-oxidation protein genes, a system based on the yeast Saccharomyces cerevisiae has been developed. We plan to clone novel C. elegans open reading frames postulated to encode ?-oxidation enzymes; to produce these novel proteins and enzymatically characterise them; to clarify their subcellular location using reporter proteins expressed in yeast cells; to demonstrate a physiological function of these novel nematode proteins by expressing them in appropriate yeast mutants and monitor functional complementation

Research institution(s)
  • Universität Wien - 100%

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