Multifunctional properties of plant proteins: citoplasmic glyceraldehyde-3-phosphate dehydrogenase as a moonlighting protein

Srakočić, Sanja (2016) Multifunctional properties of plant proteins: citoplasmic glyceraldehyde-3-phosphate dehydrogenase as a moonlighting protein. Bachelor's thesis, Faculty of Science > Department of Biology.

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Abstract

Plant cytoplasmic glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is enzyme involved in glycolysis that uses NAD+ as a cofactor. The most important catalytic residue is Cys-154. Apart from its role in glycolysis, plant citoplasmic GAPDH has additional, moonlighting functions. Moonlighting functions are regulated by post-translational redox modifications of catalytic Cys residue which inhibits GAPDH enzymatic activity. In physiological conditions the thiol group of the catalytic Cys is deprotonated which makes it strog nucleophil that can undergo redox modifications. The most common redox modifications are S-nitrosylation, glutathionylation and oxidation. There are two types of redox modifications: reversible and irreversible. Moonlighting functions of plant cytoplasmic GAPDH are triggered by reversible redox modifications. Oxidizing conditions in plant cell cause changes in subcellular localization. Citoplasmic GAPDH can translocate into nucleus, associate with outer membrane of mitochondria, plasma membrane or cytoskeleton. Citoplasmic GAPDH can also associate with other proteins and form protein complexes. In contrast with the well established moonlighting functions of animal GAPDH, little is known about moonlighting properties of plant citoplasmic GAPDH. The aim of this review is to summarize previous research and provide an insight into regulation of moonlighting properties of plant citoplasmic GAPDH.

Item Type: Thesis (Bachelor's thesis)
Supervisor: Balen, Biljana
Date: 2016
Number of Pages: 20
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Palma Dizdarevic
Date Deposited: 11 May 2017 10:26
Last Modified: 11 May 2017 10:26
URI: http://digre.pmf.unizg.hr/id/eprint/5513

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