Chemotaxis of Leptospirillum ferrooxidans and other acidophilic chemolithotrophs: comparison with the Escherichia coli chemosensory system.
Ni2+, Fe2+ and Cu2+ 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 Ni2+, 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.
Acuña
J
J
Departamento de Bioquímica, Facultad de Medicina, Universidad de Chile, Santiago.
Rojas
J
J
Amaro
A M
AM
Toledo
H
H
Jerez
C A
CA
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D002628:Chemoreceptor Cells; D002633:Chemotaxis; D004269:DNA, Bacterial; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D029968:Escherichia coli Proteins; D007919:Leptospira / Q000235:genetics / Q000502:physiology*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D008670:Metals / Q000494:pharmacology; D008745:Methylation; D008969:Molecular Sequence Data; D011956:Receptors, Cell Surface; D012689:Sequence Homology, Nucleic Acid
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D008670:Metals; D011956:Receptors, Cell Surface; C057331:Tar protein, E coli