Key contributions of a glycolipid to membrane protein integration DOI Creative Commons
Keiko Shimamoto, Kohki Fujikawa,

Tsukiho Osawa

et al.

Proceedings of the Japan Academy Series B, Journal Year: 2024, Volume and Issue: 100(7), P. 387 - 413

Published: Jan. 1, 2024

Regulation of membrane protein integration involves molecular devices such as Sec-translocons or the insertase YidC. We have identified an integration-promoting factor in inner Escherichia coli called integrase (MPIase). Structural analysis revealed that, despite its enzyme-like name, MPIase is a glycolipid with long glycan comprising N-acetyl amino sugars, pyrophosphate linker, and diacylglycerol (DAG) anchor. Additionally, we found that DAG, minor component, blocks spontaneous integration. In this review, demonstrate how they contribute to Sec-independent bacteria using comprehensive approach including synthetic chemistry biophysical analyses. DAG unfavorable integrations by suppressing mobility core, whereas compensates for this. Moreover, plays critical roles capturing substrate prevent aggregation, attracting it surface, facilitating insertion into membrane, delivering other factors. The combination efficiently regulates proteins.

Language: Английский

Key contributions of a glycolipid to membrane protein integration DOI Creative Commons
Keiko Shimamoto, Kohki Fujikawa,

Tsukiho Osawa

et al.

Proceedings of the Japan Academy Series B, Journal Year: 2024, Volume and Issue: 100(7), P. 387 - 413

Published: Jan. 1, 2024

Regulation of membrane protein integration involves molecular devices such as Sec-translocons or the insertase YidC. We have identified an integration-promoting factor in inner Escherichia coli called integrase (MPIase). Structural analysis revealed that, despite its enzyme-like name, MPIase is a glycolipid with long glycan comprising N-acetyl amino sugars, pyrophosphate linker, and diacylglycerol (DAG) anchor. Additionally, we found that DAG, minor component, blocks spontaneous integration. In this review, demonstrate how they contribute to Sec-independent bacteria using comprehensive approach including synthetic chemistry biophysical analyses. DAG unfavorable integrations by suppressing mobility core, whereas compensates for this. Moreover, plays critical roles capturing substrate prevent aggregation, attracting it surface, facilitating insertion into membrane, delivering other factors. The combination efficiently regulates proteins.

Language: Английский

Citations

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