Glycolipid MPIase is essential for the TAT (Twin-Arginine Translocation) pathway
- 1Iwate University
Abstract
TAT (Twin-Arginine Translocation) is a preprotein translocation system dedicated to membrane translocation of prefolded proteins in plants and bacteria. The TAT translocon, consisting of the TatABC subunits, drives translocation using proton motive force. However, there have been no reports on the successful reconstitution of the TAT system. In this report, we show that MPIase, a glycolipid that has been known to catalyze membrane protein integration, is essential for the TAT system. Our findings in recombinant Escherichia coli demonstrate that overproducing TatABC increases MPIase levels and that depleting MPIase results in TAT precursor accumulation in the cytosol. Furthermore, co-reconstitution of MPIase with TatABC revealed the translocation activities of TAT substrates in a proton motive force-dependent manner. This is the first successful reconstitution of the TAT system and will be advantageous for understanding its mechanisms.
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BibTeX
@misc{nishikawa2026glycolipid,
title = {{Glycolipid MPIase is essential for the TAT (Twin-Arginine Translocation) pathway}},
author = {H. Nishikawa and N. Yamamoto and H. Kunezaki and Y. Shirogane and K. Kanno and K. Sawasato and M. Yamada and K.-i. Nishiyama},
howpublished = {bioRxiv},
year = {2026},
month = jun,
doi = {10.64898/2026.06.05.730299},
url = {https://www.biorxiv.org/content/10.64898/2026.06.05.730299v4},
note = {CC BY},
}
RIS
TY - UNPB
TI - Glycolipid MPIase is essential for the TAT (Twin-Arginine Translocation) pathway
AU - H. Nishikawa
AU - N. Yamamoto
AU - H. Kunezaki
AU - Y. Shirogane
AU - K. Kanno
AU - K. Sawasato
AU - M. Yamada
AU - K.-i. Nishiyama
PY - 2026
DA - 2026/06/05
PB - bioRxiv
DO - 10.64898/2026.06.05.730299
UR - https://www.biorxiv.org/content/10.64898/2026.06.05.730299v4
AB - TAT (Twin-Arginine Translocation) is a preprotein translocation system dedicated to membrane translocation of prefolded proteins in plants and bacteria. The TAT translocon, consisting of the TatABC subunits, drives translocation using proton motive force. However, there have been no reports on the successful reconstitution of the TAT system. In this report, we show that MPIase, a glycolipid that has been known to catalyze membrane protein integration, is essential for the TAT system. Our findings in recombinant Escherichia coli demonstrate that overproducing TatABC increases MPIase levels and that depleting MPIase results in TAT precursor accumulation in the cytosol. Furthermore, co-reconstitution of MPIase with TatABC revealed the translocation activities of TAT substrates in a proton motive force-dependent manner. This is the first successful reconstitution of the TAT system and will be advantageous for understanding its mechanisms.
ER -