Taferner 2015 PLoS One

From Bioblast
Jump to navigation Jump to search
Publications in the MiPMap
Taferner A, Pircher H, Koziel R, von Grafenstein S, Baraldo G, Palikaras K, Liedl KR, Tavernarakis N, Jansen-Dürr P (2015) FAH domain containing protein 1 (FAHD-1) is required for mitochondrial function and locomotion activity in C. elegans. PLoS One 10(8):e0134161.

» PMID: 26266933 Open Access

Taferner A, Pircher H, Koziel R, von Grafenstein S, Baraldo G, Palikaras K, Liedl KR, Tavernarakis N, Jansen-Duerr P (2015) PLoS One

Abstract: The fumarylacetoacetate hydrolase (FAH) protein superfamily of metabolic enzymes comprises a diverse set of enzymatic functions, including ß-diketone hydrolases, decarboxylases, and isomerases. Of note, the FAH superfamily includes many prokaryotic members with very distinct functions that lack homologs in eukaryotes. A prokaryotic member of the FAH superfamily, referred to as Cg1458, was shown to encode a soluble oxaloacetate decarboxylase (ODx). Based on sequence homologies to Cg1458, we recently identified human FAH domain containing protein-1 (FAHD1) as the first eukaryotic oxaloacetate decarboxylase. The physiological functions of ODx in eukaryotes remain unclear. Here we have probed the function of fahd-1, the nematode homolog of FAHD1, in the context of an intact organism. We found that mutation of fahd-1 resulted in reduced brood size, a deregulation of the egg laying process and a severe locomotion deficit, characterized by a reduced frequency of body bends, reduced exploratory movements and reduced performance in an endurance exercise test. Notably, mitochondrial function was altered in the fahd-1(tm5005) mutant strain, as shown by a reduction of mitochondrial membrane potential and a reduced oxygen consumption of fahd-1(tm5005) animals. Mitochondrial dysfunction was accompanied by lifespan extension in worms grown at elevated temperature; however, unlike in mutant worms with a defect in the electron transport chain, the mitochondrial unfolded protein response was not upregulated in worms upon inactivation of fahd-1. Together these data establish a role of fahd-1 to maintain mitochondrial function and consequently physical activity in nematodes.


O2k-Network Lab: AT Innsbruck Jansen-Duerr P


Labels: MiParea: Respiration, Genetic knockout;overexpression, Comparative MiP;environmental MiP 


Organism: Caenorhabditis elegans, Nematodes 

Preparation: Intact organism 


Coupling state: ROUTINE 

HRR: Oxygraph-2k