D'Enfert C, Pugsley A P
Unité de Génétique Moléculaire, Institut Pasteur, Paris, France.
J Bacteriol. 1989 Jul;171(7):3673-9. doi: 10.1128/jb.171.7.3673-3679.1989.
The product of the Klebsiella pneumoniae gene pulS, which is located downstream from the pullulanase structural gene (pulA), is essential for the cell surface localization and extracellular release of pullulanase in Escherichia coli K-12. pulS is transcribed in the opposite direction to pulA, from which it is separated by a region of 624 nucleotides. Although this latter region contains a new component of the maltose regulon, pulB, which is transcribed from the pulA promoter, it is not required for pullulanase synthesis or secretion. Unlike pulA and all other pullulanase secretion genes characterized so far, the expression of pulS is not induced by growth in the presence of maltose and is unaffected by mutations in the maltose regulator gene malT. The pulS gene product was identified as a ca. 12-kilodalton outer membrane lipoprotein. The characterization of PulS brings to three the number of identified proteins which are known to be required for pullulanase secretion in addition to the components of the signal sequence-dependent general protein export pathway.
肺炎克雷伯菌基因pulS位于支链淀粉酶结构基因(pulA)的下游,其产物对于支链淀粉酶在大肠杆菌K - 12中的细胞表面定位和胞外释放至关重要。pulS的转录方向与pulA相反,二者之间被一个624个核苷酸的区域隔开。尽管后一个区域包含麦芽糖调节子的一个新组分pulB,它由pulA启动子转录,但支链淀粉酶的合成或分泌并不需要它。与pulA以及迄今已鉴定的所有其他支链淀粉酶分泌基因不同,pulS的表达不会因在麦芽糖存在下生长而被诱导,并且不受麦芽糖调节基因malT突变的影响。pulS基因产物被鉴定为一种约12千道尔顿的外膜脂蛋白。除了信号序列依赖性一般蛋白质输出途径的组分外,PulS的特性使已知支链淀粉酶分泌所需的已鉴定蛋白质数量增至三种。