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S A Yankofsky

Publications and source records attributed to S A Yankofsky.

12 recordsLinked to original sources

The presence of complete but masked freezing nuclei in various artificially constructed ice nucleation-active proteobacteria.

Disparate gamma-subdivision proteobacteria artificially endowed with the same ice gene of enteric origin acquired water-freezing potential at -12 degrees C, but expressed it to varying extents under identical conditions of culture as well as after being subjected to certain post-culture treatments. Varying rates of cell-bound ice nucleus synthesis were probably not the root cause of these observed interspecies differences in nucleation-active cell frequency because potentially functional but masked ice-forming templates were found in the outer cell envelope of even initially inactive individuals taken from physiologically uniform populations of virtually all tested species. We therefore propose that the extent of bacterial ice nucleation generally reflects species-specified extent of ice nucleus sequestration.

Anti-Bacterial Agents↗

Genetic transformation of obligately chemolithotrophic thiobacilli.

Genetic transformation of Thiobacaillus thioparus auxotrophs to prototrophy was obtained at frequencies of up to 10(-2) when proliferating cell populations were exposed to chromosomal DNA from a nutritionally independent strain of the same bacterium. The rate at which transformation occurred depended on recipient growth rate and could be drastically reduced by depriving otherwise competent cells of either nitrogen or exogenous energy substrate. Interspecies marker transfer was also shown among several obligately chemolithotrophic members of the genus.

Genetic Markers↗

Active transport of amino acids in Thiobacillus thioparus is a low-affinity process.

A method for the isolation of amino acid auxotrophs of Thiobacillus thioparus is described. Characterization of a leucine auxotroph indicated that leucine biosynthesis in T. thioparus was not different from that of heterotrophic bacteria. T. thioparus cells accumulated amino acids via an active mechanism. Kt values of amino acid transport were between 15 and 330 microM, and Vmax values were 200 to 350 pmol min-1 mg of protein-1. Amino acid transport was carried out by a limited number of systems, each responsible for the uptake of several amino acids. Amino acid auxotrophs of T. thioparus exhibited transport and growth properties similar to those of transport-deficient mutants of heterotrophs which lost the high-affinity, but retained the low-affinity, amino acid transport systems.

Amino Acids↗

Regulation of amino acid transport in Thiobacillus thioparus.

Amino acid transport in amino acid auxotrophs of Thiobacillus thioparus was enhanced during growth on rate-limiting amino acid concentration. A pleiotropic mutation enhanced general amino acid transport as manifested by higher values of Vmax of amino acid transport. Affinity constants remained unaltered. Mutants with enhanced transport properties did not show changes in oxidation of thiosulfate, did not oxidize various organic compounds, and did not increase the heterotrophic potential of T. thioparus. The mutations for enhanced transport caused increased synthesis of amino acid transport system components. A method for genetic transformation of T. thioparus is described.

Amino Acids↗