1887

Abstract

The Gram-positive bacteria ISO-5 and sp. RHA1 utilized taurine (2-aminoethanesulfonate) as the sole source of carbon or of nitrogen or of sulfur for growth. Different gene clusters and enzymes were active under these different metabolic situations. Under carbon- or nitrogen-limited conditions three enzymes were induced, though to different levels: taurine-pyruvate aminotransferase (Tpa), alanine dehydrogenase (Ald) and sulfoacetaldehyde acetyltransferase (Xsc). The specific activities of these enzymes in ISO-5 were sufficient to explain the growth rates under the different conditions. These three enzymes were purified and characterized, and the nature of each reaction was confirmed. Analyses of the genome of sp. RHA1 revealed a gene cluster, , putatively encoding regulation and oxidation of taurine, located 20 kbp from the gene and separate from two candidate phosphotransacetylase () genes, as well as many candidate ABC transporters (). PCR primers allowed the amplification and sequencing of the gene cluster and the gene in ISO-5. The N-terminal sequences of the three tested proteins matched the derived amino acid sequences of the corresponding genes. The sequences of the four genes found in each strain shared high degrees of identity (>95 % identical positions). RT-PCR studies proved transcription of the gene when taurine was the source of carbon or of nitrogen. Under sulfur-limited conditions no mRNA was generated and no Xsc was detected. Taurine dioxygenase (TauD), the enzyme catalysing the anticipated desulfonative reaction when taurine sulfur is assimilated, was presumed to be present because oxygen-dependent taurine disappearance was demonstrated with taurine-grown cells only. A putative gene (with three other candidates) was detected in strain ISO-5. Regulation of the different forms of metabolism of taurine remains to be elucidated.

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2004-06-01
2019-12-12
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