Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol.

Sankaran, Krishnan; Wu, Henry C.

doi:10.1016/s0021-9258(17)32077-x

Cited by 338 publications

(57 citation statements)

References 32 publications

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“…In bacteria, PG is used as a substrate for the lipidation of lipoproteins [ 37 ]. In cyanobacteria, several lumenal proteins such as CyanoP and CyanoQ, homologs of PsbP and PsbQ in land plants, are modified by diacylglycerol and palmitate [ 38 ].…”

Section: Discussionmentioning

confidence: 99%

Specific Incorporation of Polyunsaturated Fatty Acids into the sn-2 Position of Phosphatidylglycerol Accelerates Photodamage to Photosystem II under Strong Light

Jimbo

Yuasa

Takagi

et al. 2021

IJMS

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Free fatty acids (FFAs) are generated by the reaction of lipases with membrane lipids. Generated polyunsaturated fatty acids (PUFAs) containing more than two double bonds have toxic effects in photosynthetic organisms. In the present study, we examined the effect of exogenous FFAs in the growth medium on the activity of photosystem II (PSII) under strong light in the cyanobacterium Synechocystis sp. PCC 6803 (Synechocystis). PUFAs but not monounsaturated fatty acids accelerated the rate of photodamage to PSII by inactivating electron transfer at the oxygen-evolving complex. Moreover, supplemented PUFAs were specifically incorporated into the sn-2 position of phosphatidylglycerol (PG), which usually contains C16 fatty acids at the sn-2 position in Synechocystis cells. The disruption of the gene for an acyl-ACP synthetase reduced the effect of PUFAs on the photoinhibition of PSII. Thus, the specific incorporation of PUFAs into PG molecules requires acyl-ACP synthetase and leads to an unstable PSII, thereby accelerating photodamage to PSII. Our results are a breakthrough into elucidating the molecular mechanism of the toxicity of PUFAs to photosynthetic organisms.

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Section: Discussionmentioning

confidence: 99%

Specific Incorporation of Polyunsaturated Fatty Acids into the sn-2 Position of Phosphatidylglycerol Accelerates Photodamage to Photosystem II under Strong Light

Jimbo

Yuasa

Takagi

et al. 2021

IJMS

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“…Maturation and processing of lipoproteins takes place on the periplasmic side of IM (figure 1). The first step is the addition of diacylglycerol to the sulfhydryl group of the conserved Cys residue by phosphatidylglycerol/prolipoprotein diacylglyceryl transferase (Lgt) [10]. This modification is a prerequisite for the SS cleavage by a dedicated lipoprotein signal peptidase (LspA or signal peptidase II) [2,11,12] and ensures that the apolipoprotein remains anchored in the IM after SS cleavage.…”

Section: Lipoprotein Maturation and Processingmentioning

confidence: 99%

Outer membrane lipoprotein biogenesis: Lol is not the end

Konovalova¹,

Silhavy²

2015

Phil. Trans. R. Soc. B

118

111

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Bacterial lipoproteins are lipid-anchored proteins that contain acyl groups covalently attached to the N-terminal cysteine residue of the mature protein. Lipoproteins are synthesized in precursor form with an N-terminal signal sequence (SS) that targets translocation across the cytoplasmic or inner membrane (IM). Lipid modification and SS processing take place at the periplasmic face of the IM. Outer membrane (OM) lipoproteins take the localization of lipoproteins (Lol) export pathway, which ends with the insertion of the N-terminal lipid moiety into the inner leaflet of the OM. For many lipoproteins, the biogenesis pathway ends here. We provide examples of lipoproteins that adopt complex topologies in the OM that include transmembrane and surface-exposed domains. Biogenesis of such lipoproteins requires additional steps beyond the Lol pathway. In at least one case, lipoprotein sequences reach the cell surface by being threaded through the lumen of a beta-barrel protein in an assembly reaction that requires the heteropentomeric Bam complex. The inability to predict surface exposure reinforces the importance of experimental verification of lipoprotein topology and we will discuss some of the methods used to study OM protein topology.

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“…All reside in the cytoplasmic membrane and all have active sites facing the periplasm. The first enzyme, lipoprotein diacylglyceryltransferase, Lgt, transfers a diacylglyceryl (DAG) moiety from a phospholipid, usually phosphatidylglycerol, PG, to a conserved cysteine in the membrane-anchored signal peptide of a preproBLP 12 . The lipid and the protein are in thioether linkage and the modification produces a proBLP that is now doubly anchored in the membrane.…”

Section: Introductionmentioning

confidence: 99%

Structural basis of the membrane intramolecular transacylase reaction responsible for lyso-form lipoprotein synthesis

et al. 2021

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Lipoproteins serve diverse functions in the bacterial cell and some are essential for survival. Some lipoproteins are adjuvants eliciting responses from the innate immune system of the host. The growing list of membrane enzymes responsible for lipoprotein synthesis includes the recently discovered lipoprotein intramolecular transacylase, Lit. Lit creates a lipoprotein that is less immunogenic, possibly enabling the bacteria to gain a foothold in the host by stealth. Here, we report the crystal structure of the Lit enzyme from Bacillus cereus and describe its mechanism of action. Lit consists of four transmembrane helices with an extracellular cap. Conserved residues map to the cap-membrane interface. They include two catalytic histidines that function to effect unimolecular transacylation. The reaction involves acyl transfer from the sn-2 position of the glyceryl moiety to the amino group on the N-terminal cysteine of the substrate via an 8-membered ring intermediate. Transacylation takes place in a confined aromatic residue-rich environment that likely evolved to bring distant moieties on the substrate into proximity and proper orientation for catalysis.

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Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol.

Cited by 338 publications

References 32 publications

Specific Incorporation of Polyunsaturated Fatty Acids into the sn-2 Position of Phosphatidylglycerol Accelerates Photodamage to Photosystem II under Strong Light

Specific Incorporation of Polyunsaturated Fatty Acids into the sn-2 Position of Phosphatidylglycerol Accelerates Photodamage to Photosystem II under Strong Light

Outer membrane lipoprotein biogenesis: Lol is not the end

Structural basis of the membrane intramolecular transacylase reaction responsible for lyso-form lipoprotein synthesis

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