Chemotaxis of Leptospirillum ferrooxidans and other acidophilic chemolithotrophs: comparison with the Escherichia coli chemosensory system

• Published in: FEMS microbiology letters 1992-09, Vol.96 (1), p.37-42
• Main Authors: Acuña, J., Rojas, J., Amaro, A.M., Toledo, H., Jerez, C.A.
• Format: Article
• Language: English
• Subjects: Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Base Sequence; Chemoreceptor Cells; Chemosensory system; Chemotaxis; DNA, Bacterial; Electrophoresis, Polyacrylamide Gel; Escherichia coli - genetics; Escherichia coli - physiology; Escherichia coli Proteins; Leptospira - genetics; Leptospira - physiology; Leptospirillum ferrooxidans; Membrane Proteins - genetics; Membrane Proteins - metabolism; Metals - pharmacology; Methylation; Molecular Sequence Data; Protein methylation; Receptors, Cell Surface; Sequence Homology, Nucleic Acid; Thiobacillus ferrooxidans
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1016/0378-1097(92)90453-U

Ni 2+, Fe 2+ and Cu 2+ were attractants and aspartate was an apparent repellent for Leptospirillum ferrooxidans, a behaviour opposite to that for Escherichia coli. Membranes from L. ferrooxidans contained proteins with a molecular mass in the range of 80 kDa which were methylated in vitro. Methylation was stimulated in the presence of a membrane-free extract from E. coli, showing the response pattern expected for L. ferrooxidans, increased methylation by Ni 2+, and demethylation by aspartate. This suggests the existence of sensory transducers having a common methylation domain with the E. coli methyl-accepting chemotaxis proteins. Total chromosomal DNA digests from L. ferrooxidans, Thiobacillus ferrooxidans and T. thiooxidans hybridized with probes containing different domains of the tar gene from E. coli, implying the presence of tar type genes in the acidophilic bacteria studied.