Export of Thermus thermophilus alkaline phosphatase via the twin‐arginine translocation pathway in Escherichia coli

FEBS Letters

Gouffi, Kamila³  Berenguer, José²  Moreno, Renata²  Yamagishi, Akahiko¹  Santini, Claire-Lise³  Wu, Long-Fei³  Angelini, Sandra³ 

[1] Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-03, Japan;Centro de Biologia Moleculár ‘Severo Ochoa’, UAM-CSIC, Universidad Autónoma de Madrid, 28049 Madrid, Spain;Laboratoire de Chimie Bactérienne, UPR9043, Institut de Biologie Structurale et Microbiologie, CNRS, 31 chemin Joseph Aiguier, F-13402 Marseille Cedex 20, France

关键词: Sec;    Tat pathway;    Alkaline phosphatase;    Thermophile bacterium;    Adaptation;    Evolution;    AP;    alkaline phosphatase;    ECF;    enhanced chemifluorescence;    PhoA;    alkaline phosphatase of Escherichia coli;    PNPP;    p-nitrophenyl phosphate;    PVDF;    polyvinylidene difluoride;    Tap;    Thermus thermophilus alkaline phosphatase;    Tat;    twin-arginine translocation;   

DOI  :  10.1016/S0014-5793(01)02890-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The bacterial twin-arginine translocation (Tat) pathway is distinct from the Sec system by its remarkable capacity to export folded enzymes. To address the question whether the two systems are capable of translocating homologous enzymes catalyzing the same reaction, we cloned the tap gene encoding Thermus thermophilus alkaline phosphatase (Tap) and expressed it in Escherichia coli. Unlike the alkaline phosphatase of E. coli, which is translocated through the Sec system and then activated in the periplasm, Tap was exported exclusively via the Tat pathway and active Tap precursor was observed in the cytoplasm. These results demonstrate that two sequence and functional related enzymes are exported by distinct protein transport systems, which may play an integral role in the bacterial adaptation to their environment during the evolution.

【 授权许可】

Unknown