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A chloroplast envelope‐transfer sequence functions as an export signal in Escherichia coli
Author(s) -
Liu Yan-Yun,
Akhtar M.Kalim,
Ourmozdi Elizabeth P,
Kaderbhai Naheed,
Kaderbhai Mustak A
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01228-x
Subject(s) - signal peptide , escherichia coli , periplasmic space , transit peptide , biochemistry , peptide sequence , twin arginine translocation pathway , signal peptidase , biology , protein subunit , peptide , chloroplast , plastid , gene
The small subunit precursor of pea ribulose‐1,5‐bisphosphate carboxylase/oxygenase engineered with prokaryotic elements was expressed in Escherichia coli . This resulted in a dependable level of synthesis of the precursor protein in E. coli . The bacterially synthesised plant precursor protein was translocated from the cytoplasm and targeted to the outer membrane of the envelope zone. During the translocation step, a significant proportion of the precursor was processed to a soluble, mature SSU and found localised in the periplasm. The determined amino acid sequence of the isolated precursor showed that it had a deletion of an arginine residue at position −15 in the transit peptide. Expression of this transit peptide‐appended mammalian cytochrome b 5 in E. coli displayed a targeting profile of the chromogenic chimera that was similar to that observed with the plant precursor protein.