Characterization of recombinant cysteine synthase in Caenorhabditis elegans

 

R. Vozdek1, A. Hnizda1, J. Krijt1, M. Kodicek2, V. Kozich1

 

1 Institute of Inherited Metabolic Diseases, First Faculty of Medicine, Charles University in Prague

2 Department of Biochemistry and Mikrobiology, Faculty of Food and Biochemical Technology, Institute of Chemical Technology, Prague

 

Nematode Caenorhabditis elegans could be a suitable model to study metabolic and cellular consequences of homocystinuria due to cystathionine β-synthase (CBS) deficiency. However, metabolism of sulfur amino acids in C. elegans is as yet unknown, namely the steps in cysteine biosynthetic pathways. Cysteine can be synthesized either via the transsulfuration pathway which utilizes homocysteine by CBS or via the assimilation pathway which uses sulfide by cysteine synthase (CS).

In silico analysis of C. elegans database identified four homologs of human CBS, namely ZC373.1, C17G1.7, K10H10.2 and R08E5.2. The aim of this study was to express the gene C17G1.7 (predicted CS) in prokaryotic system, to purify and further characterize this recombinant protein. Molecular weight of polypeptide chain was determined to be 37,2 kDa by MALDI-TOF MS. Blue Native electrophoresis revealed a molecular weight of 70 kDa suggesting that recombinant CS is a dimer. Purified protein contains pyridoxal 5'-phosphate (PLP) as determined by UV/VIS absorption spectrometry; circular dichroism showed characteristic PLP maximum confirming its localization in a centre of organized globular protein. We determined that purified enzyme has very specific enzymic activity for CS reaction; other possible activities were not detected. Recombinant CS exhibited Km values for O-acetyl-L-serine and sulfide of 5.54 and 4.23 mM, respectively, and a turnover number of 139 and 134 s-1, respectively.

These data show that C17G1.7 could play an important role in cysteine biosynthesis since C. elegans genome contains also a CBS gene, we hypothesize that nematode utilizes both cysteine biosythesis pathways - sulfur assimilation and transsulfuration pathway.

 

This work was supported by Wellcome trust International senior research fellowship in  biomedical science in central europe