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Updated: Aug 15, 2026
Super-Resolution Microscopy of the Synaptonemal Complex Within the Caenorhabditis elegans Germline
Published on: September 13, 2022
Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans
Veronica T Dufe1, Kai Lüersen, Marie-Luise Eschbach
1Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, 221 00 Lund, Sweden.
Abstract:
The polyamine synthesis enzyme spermidine synthase (SPDS) has been cloned from the model nematode Caenorhabditis elegans. Biochemical characterisation of the recombinantly expressed protein revealed a high degree of similarity to other eukaryotic SPDS with the exception of a low affinity towards the substrate decarboxylated S-adenosylmethionine (Km = 110 microM) and a less pronounced feedback inhibition by the second reaction product 5'-methylthioadenosine (IC50 = 430 microM). The C. elegans protein that carries a nematode-specific insertion of 27 amino acids close to its N-terminus was crystallized, leading to the first X-ray structure of a dimeric eukaryotic SPDS.
