Email updates

Keep up to date with the latest news and content from BMC Genomics and BioMed Central.

Open Access Research article

Clostridium sticklandii, a specialist in amino acid degradation:revisiting its metabolism through its genome sequence

Nuria Fonknechten123, Sébastien Chaussonnerie123, Sabine Tricot123, Aurélie Lajus123, Jan R Andreesen5, Nadia Perchat123, Eric Pelletier123, Michel Gouyvenoux123, Valérie Barbe123, Marcel Salanoubat123, Denis Le Paslier123, Jean Weissenbach123, Georges N Cohen4 and Annett Kreimeyer123*

Author Affiliations

1 CEA, DSV, Institut de Génomique, Genoscope, 2 rue Gaston Crémieux, F-91057 Evry, France

2 CNRS-UMR 8030 F-91057 Evry, France

3 UEVE, Université d'Evry, F-91057 Evry, France

4 Institut Pasteur, 28 rue du Dr. Roux, F-75724 Paris cedex 15, France

5 Institute of Biology/Microbiology, University of Halle, Kurt-Mothes-Str. 3, D-06120 Halle, Germany

For all author emails, please log on.

BMC Genomics 2010, 11:555  doi:10.1186/1471-2164-11-555

Published: 11 October 2010

Abstract

Background

Clostridium sticklandii belongs to a cluster of non-pathogenic proteolytic clostridia which utilize amino acids as carbon and energy sources. Isolated by T.C. Stadtman in 1954, it has been generally regarded as a "gold mine" for novel biochemical reactions and is used as a model organism for studying metabolic aspects such as the Stickland reaction, coenzyme-B12- and selenium-dependent reactions of amino acids. With the goal of revisiting its carbon, nitrogen, and energy metabolism, and comparing studies with other clostridia, its genome has been sequenced and analyzed.

Results

C. sticklandii is one of the best biochemically studied proteolytic clostridial species. Useful additional information has been obtained from the sequencing and annotation of its genome, which is presented in this paper. Besides, experimental procedures reveal that C. sticklandii degrades amino acids in a preferential and sequential way. The organism prefers threonine, arginine, serine, cysteine, proline, and glycine, whereas glutamate, aspartate and alanine are excreted. Energy conservation is primarily obtained by substrate-level phosphorylation in fermentative pathways. The reactions catalyzed by different ferredoxin oxidoreductases and the exergonic NADH-dependent reduction of crotonyl-CoA point to a possible chemiosmotic energy conservation via the Rnf complex. C. sticklandii possesses both the F-type and V-type ATPases. The discovery of an as yet unrecognized selenoprotein in the D-proline reductase operon suggests a more detailed mechanism for NADH-dependent D-proline reduction. A rather unusual metabolic feature is the presence of genes for all the enzymes involved in two different CO2-fixation pathways: C. sticklandii harbours both the glycine synthase/glycine reductase and the Wood-Ljungdahl pathways. This unusual pathway combination has retrospectively been observed in only four other sequenced microorganisms.

Conclusions

Analysis of the C. sticklandii genome and additional experimental procedures have improved our understanding of anaerobic amino acid degradation. Several specific metabolic features have been detected, some of which are very unusual for anaerobic fermenting bacteria. Comparative genomics has provided the opportunity to study the lifestyle of pathogenic and non-pathogenic clostridial species as well as to elucidate the difference in metabolic features between clostridia and other anaerobes.