Fortin Y, Phoenix P, Drapeau G R
Department of Microbiology and Immunology, Université de Montréal, Québec, Canada.
J Bacteriol. 1990 Nov;172(11):6607-10. doi: 10.1128/jb.172.11.6607-6610.1990.
Mutant strains of Escherichia coli were screened for the ability to grow on L agar plates containing 3.4 or 4.6 mM sodium azide. Most mutants had mutations located in the leucine region, presumably at the azi locus. Two of these mutants were found to have a mutation in the secA gene, but expression of the resistance phenotype also required the presence of upstream gene X. While a plasmid carrying the X-secA mutant gene pair was able to confer azide resistance to a sensitive host, a similar plasmid harboring the wild-type secA allele rendered a resistant strain sensitive to azide, indicating codominance of the two alleles. That azide inhibits SecA is consistent with the fact that SecA has ATPase activity, an activity that is often prone to inhibition by azide.
筛选大肠杆菌突变株,以检测其在含有3.4或4.6 mM叠氮化钠的L琼脂平板上生长的能力。大多数突变体的突变位于亮氨酸区域,推测位于azi位点。发现其中两个突变体在secA基因中有突变,但抗性表型的表达还需要上游基因X的存在。虽然携带X-secA突变基因对的质粒能够赋予敏感宿主叠氮化物抗性,但携带野生型secA等位基因的类似质粒使抗性菌株对叠氮化物敏感,表明这两个等位基因共显性。叠氮化物抑制SecA这一现象与SecA具有ATP酶活性这一事实相符,而ATP酶活性通常容易受到叠氮化物的抑制。