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Transport of cytochrome c derivatives by the bacterial Tat protein translocation system
Author(s) -
Sanders Carsten,
Wethkamp Nils,
Lill Holger
Publication year - 2001
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2001.02514.x
Subject(s) - periplasmic space , cytoplasm , biology , signal peptide , biochemistry , transport protein , twin arginine translocation pathway , membrane transport protein , escherichia coli , bacterial outer membrane , protein folding , microbiology and biotechnology , translocon , folding (dsp implementation) , peptide , heterologous , membrane protein , membrane , peptide sequence , electrical engineering , gene , engineering
An experimental system developed previously for the heterologous expression of c ‐type cytochromes in Escherichia coli Q1has been adapted to monitor protein transfer across the bacteria's cytoplasmic membrane. Apocytochrome, lacking the haem cofactor and probably in an unfolded state, was readily transferred across the cytoplasmic membrane when fused to a Sec‐specific signal peptide. Furthermore, cytochrome fused to a signal peptide regarded as specific for the twin arginine transport (Tat) system was translocated in an unfolded state by the Sec apparatus. After maturation and folding in the cytoplasm, Tat‐mediated transfer of holocytochrome to the periplasm occurred. We conclude that, in addition to the nature of the specific signal peptide, the folding state of a particular protein also governs its acceptance by a given transport system.