Anderson C M, Gray J
Botany School, University of Cambridge, UK.
FEBS Lett. 1991 Mar 25;280(2):383-6. doi: 10.1016/0014-5793(91)80337-3.
Leader peptidase from Escherichia coli was able to process the precursor of pea cytochrome f synthesised in vitro. N-Terminal sequencing established that cleavage by leader peptidase generated the same mature sequence as in pea chloroplasts. Processing by leader peptidase was much more efficient co-translationally rather than post-translationally, and the extent of post-translational processing declined with time suggesting that the cytochrome f precursor folded to an uncleavable conformation. Detergent extracts of pea thylakoid membranes were unable to process the cytochrome f precursor co- or post-translationally.
来自大肠杆菌的前导肽酶能够加工体外合成的豌豆细胞色素f的前体。N端测序表明，前导肽酶的切割产生了与豌豆叶绿体中相同的成熟序列。前导肽酶的加工在共翻译时比翻译后更有效，并且翻译后加工的程度随时间下降，这表明细胞色素f前体折叠成了不可切割的构象。豌豆类囊体膜的去污剂提取物在共翻译或翻译后都无法加工细胞色素f前体。
