CHARACTERIZATION OF A TN551-MUTANT OF STAPHYLOCOCCUS-AUREUS DEFECTIVE IN THE PRODUCTION OF SEVERAL EXOPROTEINS
CHARACTERIZATION OF A TN551-MUTANT OF STAPHYLOCOCCUS-AUREUS DEFECTIVE IN THE PRODUCTION OF SEVERAL EXOPROTEINS
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DOI：
10.1139/m94-107
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发表时间：
1994-08-01
影响因子：
2.8
通讯作者：
NAGEL, R
中科院分区：
文献类型：
--
作者：
GIRAUDO, AT;RASPANTI, CG;NAGEL, R
从金黄色葡萄球菌196 E中分离出一种Tn 551插入多效性突变体，该突变体在几种外蛋白的产生中有缺陷，并进行了表征。该突变体的多效性是由于转座子的单一插入，如Southern印迹杂交所证明的，并通过转导到S.金黄色葡萄球菌ISP 479。突变体显示肉汤培养物上清液中α-和β-溶血素、DNA酶、凝固酶和蛋白A水平降低或为零。蛋白酶、脂肪酶、葡激酶或肠毒素A的产生没有改变。突变体确实合成了蛋白A的细胞结合形式以及由pRIT 11编码的该蛋白的细胞外形式，pRIT 11缺乏该分子的COOH末端片段。这些观察结果表明，sae位点不涉及一个积极的调控基因在转录水平上发挥作用。该突变体的表型与其他影响外蛋白合成的插入突变体（如agr、xpr或sar）不同。这种新的突变已被指定为sae（为S。金黄色葡萄球菌外蛋白表达）。
A Tn551 insertional pleiotropic mutant defective in the production of several exoproteins was isolated from Staphylococcus aureus 196E and characterized. The pleiotropism of the mutant was due to a single insertion of the transposon as evidenced by Southern blot hybridization and by the transfer of its phenotype by transduction to S. aureus ISP479. The mutants showed diminished or null levels of alpha- and beta-hemolysins, DNase, coagulase, and protein A in the supernatants of broth cultures. Production of proteases, lipase, staphylokinase, or enterotoxin A was not modified. The mutants did synthesize the cell-bound form of protein A and also the extracellular form of this protein coded by pRIT11, which lacks the COOH-terminal segment of the molecule. These observations suggest that the sae locus does not involve a positive regulatory gene acting at the transcriptional level. The phenotype of the mutant was different from that of other insertional mutants affecting exoprotein synthesis, such as agr, xpr, or sar. This new mutation has been designated sae (for S. aureus exoprotein expression).