Bolla J M, Lazdunski C, Inouye M, Pagès J M
Centre de Biochimie et de Biologie Moléculaire du CNRS 31 Chemin Joseph Aiguier, Marseille, France.
FEBS Lett. 1987 Nov 16;224(1):213-8. doi: 10.1016/0014-5793(87)80450-7.
The export of beta-lactamase to the periplasm of Escherichia coli can be directed by the OmpA signal peptide in the secretion cloning vector pIN-III. The overproduction of the hybrid precursor specifically induces a delay in the onset of processing of newly synthesized polypeptide chains. However, when the processing starts, no alteration in the rate of cleavage itself is observed. Our results suggest that the temporal mode of processing (which reflects translocation) does not depend on the nature of the signal peptide but rather depends on the nature of the polypeptide chain exported.
在分泌克隆载体pIN-III中，β-内酰胺酶向大肠杆菌周质的输出可由OmpA信号肽引导。杂交前体的过量产生特异性地诱导新合成多肽链加工起始的延迟。然而，当加工开始时，未观察到切割速率本身的改变。我们的结果表明，加工的时间模式（反映转运）不取决于信号肽的性质，而是取决于输出的多肽链的性质。
