YnbB is a CdsA paralogue dedicated to biosynthesis of glycolipid MPIase involved in membrane protein integration

Sato, Ryo; Sawasato, Katsuhiro; Nishiyama, Kenichi

doi:10.1016/j.bbrc.2019.01.145

Cited by 18 publications

(23 citation statements)

References 24 publications

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“…2A) (Sawasato et al, 2019a), reflecting the difference in subcellular localization. The first step of MPIase biosynthesis is catalyzed by CdsA/YnbB, a CDP-DAG synthase, through incorporation of GlcNAc-phosphate into CDP-DAG (Sato et al, 2019;Sawasato et al, 2019a).…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of glycolipid MPIase (membrane protein integrase) is independent of the genes for ECA (enterobacterial common antigen)

Kamemoto

Funaba

Kawakami

et al. 2020

J. Gen. Appl. Microbiol.

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Section: Introductionmentioning

confidence: 99%

Biosynthesis of glycolipid MPIase (membrane protein integrase) is independent of the genes for ECA (enterobacterial common antigen)

Kamemoto

Funaba

Kawakami

et al. 2020

J. Gen. Appl. Microbiol.

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“…At an early stage after the temperature downshift, promoter P5 acts, and then promoter P3 begins to act so that the cdsA expression and therefore the MPIase expression is kept high in the cold. While ynbB , a paralogue of cdsA , is also involved in the increase in the MPIase level in the cold, the effect is weak and marginal . Therefore, the effect of ynbB is a backup of that of cdsA .…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

“…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 . MPIase is composed of a linear glycan chain comprising 9‐11 repeats of the trisaccharide unit of N ‐acetyl‐D‐glucosamine (GlcNAc), N ‐acetyl‐D‐mannosaminuronic acid and 4‐acetoamido‐4‐deoxy‐D‐fucose, and diacylglycerol through a pyrophosphate linker .…”

mentioning

confidence: 99%

“…GlcNAc‐P is substituted by the CMP moiety of CDP‐DAG on CdsA, giving Compound I . 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 .…”

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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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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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YnbB is a CdsA paralogue dedicated to biosynthesis of glycolipid MPIase involved in membrane protein integration

Cited by 18 publications

References 24 publications

Biosynthesis of glycolipid MPIase (membrane protein integrase) is independent of the genes for ECA (enterobacterial common antigen)

Biosynthesis of glycolipid MPIase (membrane protein integrase) is independent of the genes for ECA (enterobacterial common antigen)

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

Structural Requirements of a Glycolipid MPIase for Membrane Protein Integration

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