Real time analysis of lipoprotein transfer from LolA to LolB by means of surface plasmon resonance

Tsukahara, Jun; Narita, Shin‐ichiro; Tokuda, Harukuni

doi:10.1016/j.febslet.2009.08.032

Cited by 3 publications

(2 citation statements)

References 15 publications

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“…Xcc LolA and LolB forms a stable complex in solution in the absence of lipoprotein Our results from SEC and ITC analyses show that Xcc LolA and a periplasmic variant of LolB form a 1:1 complex in solution in the absence of bound lipoprotein (LP). For E. coli LolB, a periplasmic version (mLolB) was able to successfully accept lipoprotein cargo from LolA but caused mislocalization of OM lipoproteins to the inner membrane (Tsukahara et al, 2009). Thus, at least in E. coli, the absence of the tether peptide does not appear to influence lipid binding or transfer between the two proteins.…”

Section: Discussionmentioning

confidence: 99%

LolA and LolB from the plant-pathogen Xanthomonas campestris forms a stable heterodimeric complex in the absence of lipoprotein

Furlanetto

Divne

2023

Front. Microbiol.

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The Gram-negative bacterium Xanthomonas campestris is one of the most problematic phytopathogens, and especially the pathovar campestris (Xcc) that causes a devastating plant disease known as black rot and it is of considerable interest to understand the molecular mechanisms that enable virulence and pathogenicity. Gram-negative bacteria depend on lipoproteins (LPs) that serve many important functions including control of cell shape and integrity, biogenesis of the outer membrane (OM) and establishment of transport pathways across the periplasm. The LPs are localized to the OM where they are attached via a lipid anchor by a process known as the localization of lipoprotein (Lol) pathway. Once a lipid anchor has been synthesized on the nascent LP, the Lol pathway is initiated by a membrane-bound ABC transporter that extracts the lipid anchor of the LP from the IM. The ABC extractor presents the extracted LP to the transport protein LolA, which binds the anchor and thereby shields it from the hydrophilic periplasmic milieu. It is assumed that LolA then carries the LP across the periplasm to the OM. At the periplasmic face of the OM, the LP cargo is delivered to LolB, which completes the Lol pathway by inserting the LP anchor in the inner leaflet of the outer membrane. Earlier studies have shown that loss of Xcc LolA or LolB leads to decreased virulence and pathogenicity during plant infection, which motivates studies to better understand the Lol system in Xcc. In this study, we report the first experimental structure of a complex between LolA and LolB. The crystal structure reveals a stable LolA-LolB complex in the absence of LP. The structural integrity of the LP-free complex is safeguarded by specific protein–protein interactions that do not coincide with interactions predicted to participate in lipid binding. The results allow us to identify structural determinants that enable Xcc LolA to dock with LolB and initiate LP transfer.

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Section: Discussionmentioning

confidence: 99%

LolA and LolB from the plant-pathogen Xanthomonas campestris forms a stable heterodimeric complex in the absence of lipoprotein

Furlanetto

Divne

2023

Front. Microbiol.

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“…Lipoproteins released into the periplasm form a water-soluble complex with the perisplasmic chaperone, LolA (Remans et al, 2010). This LolA-lipoprotein complex crosses the periplasm and then interacts with the outer membrane receptor LolB, which is essential for the anchoring of lipoproteins to the outer membrane (Tsukahara et al, 2009). The Lol system has recently implicated as an alternative to the β-barrel assembly machinery (BAM) for the assembly and insertion of integral outer membrane proteins (Collin et al, 2011; Dunstan et al, 2015; Huysmans et al, 2015; Jeeves and Knowles, 2015).…”

Section: Discussionmentioning

confidence: 99%

Differential Protein Expression During Growth on Medium Versus Long-Chain Alkanes in the Obligate Marine Hydrocarbon-Degrading Bacterium Thalassolituus oleivorans MIL-1

et al. 2018

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The marine obligate hydrocarbonoclastic bacterium Thalassolituus oleivorans MIL-1 metabolizes a broad range of aliphatic hydrocarbons almost exclusively as carbon and energy sources. We used LC-MS/MS shotgun proteomics to identify proteins involved in aerobic alkane degradation during growth on medium- (n-C14) or long-chain (n-C28) alkanes. During growth on n-C14, T. oleivorans expresses an alkane monooxygenase system involved in terminal oxidation including two alkane 1-monooxygenases, a ferredoxin, a ferredoxin reductase and an aldehyde dehydrogenase. In contrast, during growth on long-chain alkanes (n-C28), T. oleivorans may switch to a subterminal alkane oxidation pathway evidenced by significant upregulation of Baeyer-Villiger monooxygenase and an esterase, proteins catalyzing ketone and ester metabolism, respectively. The metabolite (primary alcohol) generated from terminal oxidation of an alkane was detected during growth on n-C14 but not on n-C28 also suggesting alternative metabolic pathways. Expression of both active and passive transport systems involved in uptake of long-chain alkanes was higher when compared to the non-hydrocarbon control, including a TonB-dependent receptor, a FadL homolog and a specialized porin. Also, an inner membrane transport protein involved in the export of an outer membrane protein was expressed. This study has demonstrated the substrate range of T. oleivorans is larger than previously reported with growth from n-C10 up to n-C32. It has also greatly enhanced our understanding of the fundamental physiology of T. oleivorans, a key bacterium that plays a significant role in natural attenuation of marine oil pollution, by identifying key enzymes expressed during the catabolism of n-alkanes.

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The Journey of Lipoproteins Through the Cell

Szewczyk

Collet

2016

Advances in Microbial Physiology

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Real time analysis of lipoprotein transfer from LolA to LolB by means of surface plasmon resonance

Cited by 3 publications

References 15 publications

LolA and LolB from the plant-pathogen Xanthomonas campestris forms a stable heterodimeric complex in the absence of lipoprotein

LolA and LolB from the plant-pathogen Xanthomonas campestris forms a stable heterodimeric complex in the absence of lipoprotein

Differential Protein Expression During Growth on Medium Versus Long-Chain Alkanes in the Obligate Marine Hydrocarbon-Degrading Bacterium Thalassolituus oleivorans MIL-1

The Journey of Lipoproteins Through the Cell

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