Sakamoto T, Kawasaki H, Sakai T
Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University, Sakai, Japan.
FEBS Lett. 1996 Dec 2;398(2-3):269-73. doi: 10.1016/s0014-5793(96)01257-4.
The gene encoding the pectin lyase (PNL; EC 4.2.2.10) of Bacillus subtilis has been cloned, sequenced, and characterized. A coding sequence for the PNL composed of 345 amino acids including a 24-amino-acid signal peptide was assigned. No sequence resembling a LexA binding site was found upstream of the structural gene. Furthermore, PNL activity of the gene product expressed in Escherichia coli DH5alpha was detected intracellularly, which might suggest that expression of the gene was not controlled by RecA. Regulation of the gene expression seemed to be quite different from that of other bacterial PNL genes previously reported.
枯草芽孢杆菌果胶裂解酶（PNL；EC 4.2.2.10）的编码基因已被克隆、测序和表征。确定了由345个氨基酸组成的PNL编码序列，其中包括一个24个氨基酸的信号肽。在结构基因上游未发现类似LexA结合位点的序列。此外，在大肠杆菌DH5α中表达的基因产物的PNL活性在细胞内被检测到，这可能表明该基因的表达不受RecA的控制。该基因表达的调控似乎与先前报道的其他细菌PNL基因有很大不同。
