Increased expression of the bacterial glycolipid MPIase is required for efficient protein translocation across membranes in cold conditions

Sawasato, Katsuhiro; Suzuki, Shohachi; Nishiyama, Kenichi

doi:10.1074/jbc.ra119.008457

Cited by 18 publications

(19 citation statements)

References 40 publications

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“…When both the cdsA and ynbB genes on the chromosome are disrupted, the increase in the MPIase level at low temperature is repressed even if CdsA is expressed from a complementary plasmid, in which cdsA is placed under the control of the arabinose promoter. Furthermore, the expression level of CdsA is upregulated to the same extent as the increase in the MPIase level in the cold . These observations indicate that the increase in the MPIase level is regulated by the CdsA level.…”

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confidence: 65%

“…MPIase also significantly stimulates protein translocation by affecting the dimer structure of SecYEG translocase . Recently, we found that the expression level of MPIase specifically increases significantly at low temperature (<25 °C) . The increase in the MPIase level is crucial for efficient protein translocation at low temperature .…”

mentioning

confidence: 96%

“…YidC is responsible for the membrane protein integration of these proteins . The expression levels of the SecYEG translocase and YidC do not change under cold conditions . We have identified and characterized a glycolipid named MPIase (Membrane Protein Integrase), essential for membrane protein integration and therefore cell growth .…”

mentioning

confidence: 99%

“…Recently, we found that the expression level of MPIase specifically increases significantly at low temperature (<25 °C) . The increase in the MPIase level is crucial for efficient protein translocation at low temperature .…”

mentioning

confidence: 99%

“…YnbB is a CdsA paralogue dedicated to MPIase biosynthesis . Both CdsA and YnbB are involved in the increase in the MPIase level at low temperature . When both the cdsA and ynbB genes on the chromosome are disrupted, the increase in the MPIase level at low temperature is repressed even if CdsA is expressed from a complementary plasmid, in which cdsA is placed under the control of the arabinose promoter.…”

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confidence: 99%

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Two‐step induction of cdsA promoters leads to upregulation of the glycolipid MPIase at cold temperature

2019

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Glycolipid MPIase, essential for membrane protein integration into the cytoplasmic membrane of Escherichia coli, is upregulated at cold temperatures. This upregulation is rapid and sustainable. CdsA, a CDP‐diacylglycerol synthase, is a rate‐limiting enzyme for MPIase biosynthesis. Upregulation of CdsA is responsible for the increase in the MPIase level at low temperature. Investigation of cdsA regulatory regions revealed at least two cold‐inducible promoters, a cold‐shock promoter that functions transiently and immediately in the cold, and one that is sustainable in the cold. The stability of the cdsA transcript was comparable with that of tufA, which is not cold‐inducible. Thus, cdsA is induced through two‐step cold‐induction to maintain MPIase at a high level rapidly and sustainably in the cold.

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confidence: 65%

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confidence: 96%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Two‐step induction of cdsA promoters leads to upregulation of the glycolipid MPIase at cold temperature

2019

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Structural Requirements of a Glycolipid MPIase for Membrane Protein Integration

Fujikawa

Han

Osawa

et al. 2023

Chemistry A European J

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MPIase is a glycolipid involved in membrane protein integration in the inner membrane of Escherichia coli. To overcome the trace amounts and heterogeneity of natural MPIase, we systematically synthesized MPIase analogs. Structure‐activity relationship studies revealed the contribution of distinctive functional groups and the effect of the MPIase glycan length on membrane protein integration activity. In addition, both the synergistic effects of these analogs with the membrane chaperone/insertase YidC, and the chaperone‐like activity of the phosphorylated glycan were observed. These results verified the translocon‐independent membrane integration mechanism in the inner membrane of E. coli, in which MPIase captures the highly hydrophobic nascent proteins via its characteristic functional groups, prevents protein aggregation, attracts the proteins to the membrane surface, and delivers them to YidC in order to regenerate its own integration activity.

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