THE PHS GENE AND HYDROGEN-SULFIDE PRODUCTION BY SALMONELLA-TYPHIMURIUM
THE PHS GENE AND HYDROGEN-SULFIDE PRODUCTION BY SALMONELLA-TYPHIMURIUM
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DOI：
10.1128/jb.169.6.2391-2397.1987
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发表时间：
1987-06-01
影响因子：
3.2
通讯作者：
BARRETT, EL
中科院分区：
文献类型：
--
作者：
CLARK, MA;BARRETT, EL
鼠伤寒沙门氏菌从硫代硫酸盐或亚硫酸盐产生H2S。这两种还原的各自途径必须是不同的，因为携带phs、chlA和menB中的运动的突变体将亚硫酸盐还原成H2S，而不是硫代硫酸盐，并且葡萄糖抑制硫代硫酸盐产生H2S，而葡萄糖刺激其从亚硫酸盐产生。phs和chlA突变体也缺乏甲基紫精连接的硫代硫酸还原酶活性存在于厌氧生长的野生型培养物中。一些羟胺，转座子Tn 10插入，和Mu d1（四月乳糖）操纵子融合突变体缺陷的phs进行了表征。其中一种羟胺突变体是琥珀突变体，正如其突变在supD背景下受到抑制所表明的那样。温度敏感的phs突变体在30 ℃产生H2S和甲基紫精连接的硫代硫酸盐还原酶，但在42 ℃不产生。在30 ℃下生长的所有这些突变体中的还原酶与野生型酶一样热稳定，并且在电泳相对迁移率方面没有差异，这表明phs不是硫代硫酸盐还原酶的结构基因。β-的表达phs：：Mu d1（Apr lac）突变体中的半乳糖苷酶依赖于厌氧和还原硫的存在。碳源和生育期也对产量有很大影响。这个结果与phs基因编码一种调节蛋白的模型一致，该蛋白是硫代硫酸盐还原成硫化氢所必需的。
Salmonella typhimurium produces H2S from thiosulfate or sulfite. The respective pathways for the two reductions must be distinct as mutants carrying motations in phs, chlA, and menB reduced sulfite, but not thiosulfate, to H2S, and glucose repressed the production of H2S from thiosulfate while it stimulated its production from sulfite. The phs and chlA mutants also lacked a methyl viologen-linked thiosulfate reductase activity present in anaerobically grown wild-type cultures. A number of hydroxylamine, transposon Tn10 insertion, and Mu d1(Apr lac) operon fusion mutants defective in phs were characterized. One of the hydroxylamine mutants was an amber mutant, as indicated by suppression of its mutation in a supD background. The temperature-sensitive phs mutants produced H2S and methyl viologen-linked thiosulfate reductase at 30.degree.C but not at 42.degree.C. The reductases in all such mutants grown at 30.degree.C were as thermostable as the wild-type enzyme and did not differ in electrophoretic relative mobility, suggesting that phs is not the structural gene for thiosulfate reductase. Expression of .beta.-galactosidase in phs:: Mu d1 (Apr lac) mutants was dependent on anaerobiosis and the presence of reduced sulfur. It was also strongly influenced by carbon source and growth stage. The results are consistent with a model in which the phs gene encodes a regulatory protein essential for the reduction of thiosulfate to hydrogen sulfide.