Kendall K, Cullum J
Gene. 1984 Sep;29(3):315-21. doi: 10.1016/0378-1119(84)90060-x.
An extracellular agarase gene was cloned from Streptomyces coelicolor A3(2) strain M130 into S. lividans 66 using the multicopy plasmid vector pIJ702. Various deletion derivatives of the initial clone (pMT605) were obtained by in vitro and in vivo methods. This allowed the gene to be localised to a 1.9-kb segment of DNA. The agarase enzyme was overproduced (up to 500 times) and exported efficiently into the medium. The agarase protein was identified as a 28-kDal band after sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE); in the case of one derivative, pMT608, this band accounted for nearly 50% of the total extracellular protein. Differences in agarase production between the deletion derivatives correlated well with plasmid stability.
利用多拷贝质粒载体pIJ702,将来自天蓝色链霉菌A3(2)菌株M130的一个胞外琼脂酶基因克隆到变铅青链霉菌66中。通过体外和体内方法获得了初始克隆体(pMT605)的各种缺失衍生物。这使得该基因被定位到一段1.9 kb的DNA片段上。琼脂酶被过量表达(高达500倍)并有效地分泌到培养基中。经十二烷基硫酸钠(SDS)-聚丙烯酰胺凝胶电泳(PAGE)后,琼脂酶蛋白被鉴定为一条28-kDal的条带;对于一种衍生物pMT608,这条带占细胞外总蛋白的近50%。缺失衍生物之间琼脂酶产量的差异与质粒稳定性密切相关。