Detection and Characterization of a Mycobacterial L-Arabinofuranose ABC Transporter Identified with a Rapid Lipoproteomics Protocol

Li, M.; Müller, Christoph; Fröhlich, Klemens; Gorka, Oliver; Zhang, Lin; Schilling, Oliver; Einsle, Oliver; Jessen‐Trefzer, Claudia

doi:10.1016/j.chembiol.2019.03.002

Cited by 8 publications

(10 citation statements)

References 81 publications

(99 reference statements)

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“…338 Using an elegant lipoproteomics approach, one of them was recently identified as an L-arabinose importer. 343 This transporter, however, is unlikely to participate in the recycling of AG and LAM whose arabinan domains are made of D-arabinose. On the basis of its similarity with a galactose transporter of E. coli and of its clustering with genes involved with galactose metabolism, the sodium solute superfamily transporter gene galP from M. smegmatis was finally proposed to be involved in galactose recycling.…”

Section: Recycling Of Cell Envelope Constituentsmentioning

confidence: 99%

“…Compared to Mtb , the environmental saprophytic Mycobacterium species M. smegmatis potentially expresses 28 carbohydrate import systems, 19 of which are ABC transporters . Using an elegant lipoproteomics approach, one of them was recently identified as an l -arabinose importer . This transporter, however, is unlikely to participate in the recycling of AG and LAM whose arabinan domains are made of d -arabinose.…”

Section: Recycling Of Cell Envelope Constituentsmentioning

confidence: 99%

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Transporters Involved in the Biogenesis and Functionalization of the Mycobacterial Cell Envelope

et al. 2020

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The biology of mycobacteria is dominated by a complex cell envelope of unique composition and structure and of exceptionally low permeability. This cell envelope is the basis of many of the pathogenic features of mycobacteria and the site of susceptibility and resistance to many antibiotics and host defense mechanisms. This review is focused on the transporters that assemble and functionalize this complex structure. It highlights both the progress and the limits of our understanding of how (lipo)polysaccharides, (glyco)lipids, and other bacterial secretion products are translocated across the different layers of the cell envelope to their final extra-cytoplasmic location. It further describes some of the unique strategies evolved by mycobacteria to import nutrients and other products through this highly impermeable barrier.

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Section: Recycling Of Cell Envelope Constituentsmentioning

confidence: 99%

Section: Recycling Of Cell Envelope Constituentsmentioning

confidence: 99%

Transporters Involved in the Biogenesis and Functionalization of the Mycobacterial Cell Envelope

et al. 2020

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“…M. bovis BCG was grown in the presence of 1.5 mM of either trehalose (1), mannotrehalose (2) or galactotrehalose (3) for 48 h and the proteins were isolated using a modified Triton X-114 extraction protocol. 25 A list of all of the proteins identified, annotations and fold changes are in ESI List 1. † Interestingly, we did not observe any changes in proteins that are involved in trehalose uptake (LpqY) or metabolism (TreS, trehalase) indicating, importantly, that low concentrations of trehalose and modified derivatives do not alter the trehalose biosynthetic machinery of mycobacteria (ESI List 1, Fig.…”

Section: Papermentioning

confidence: 99%

Asymmetric trehalose analogues to probe disaccharide processing pathways in mycobacteria

et al. 2020

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“…Thereafter, the peptide concentration was measured using the bicinchoninic acid assay (Thermo Fisher Scientific). For MS analysis, 500 ng of peptide per sample was analyzed using the EASY-nLC Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria 1000 UHPLC system (Thermo Fisher Scientific) coupled to a Q-Exactive plus Hybrid Quadrupole-Orbitrap Mass Spectrometer (Thermo Fisher Scientific) as previously described (80). Raw data were processed and analyzed with MaxQuant (Version 1.6.0.16) using cyanobase (81) data for Synechocystis 6803 (Version 2018/08/01) including the small proteins described in reference (50).…”

Section: Methodsmentioning

confidence: 99%

Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria

Krauspe

Fahrner

Spät

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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Phycobilisomes are the major pigment–protein antenna complexes that perform photosynthetic light harvesting in cyanobacteria, rhodophyte, and glaucophyte algae. Up to 50% of the cellular nitrogen can be stored in their giant structures. Accordingly, upon nitrogen depletion, phycobilisomes are rapidly degraded following an intricate genetic program. Here, we describe the role of NblD, a cysteine-rich, small protein in this process in cyanobacteria. Deletion of the nblD gene in the cyanobacterium Synechocystis sp. PCC 6803 prevented the degradation of phycobilisomes, leading to a nonbleaching (nbl) phenotype, which could be complemented by a plasmid-localized gene copy. Competitive growth experiments between the ΔnblD and the wild-type strain provided direct evidence for the physiological importance of NblD under nitrogen-limited conditions. Ectopic expression of NblD under nitrogen-replete conditions showed no effect, in contrast to the unrelated proteolysis adaptors NblA1 and NblA2, which can trigger phycobilisome degradation. Transcriptome analysis indicated increased nblA1/2 transcript levels in the ΔnblD strain during nitrogen starvation, implying that NblD does not act as a transcriptional (co)regulator. However, immunoprecipitation and far-western experiments identified the chromophorylated (holo form) of the phycocyanin β-subunit (CpcB) as its target, while apo-CpcB was not bound. The addition of recombinant NblD to isolated phycobilisomes caused a reduction in phycocyanin absorbance and a broadening and shifting of the peak to lower wavelengths, indicating the occurrence of structural changes. These data demonstrate that NblD plays a crucial role in the coordinated dismantling of phycobilisomes and add it as a factor to the genetically programmed response to nitrogen starvation.

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Detection and Characterization of a Mycobacterial L-Arabinofuranose ABC Transporter Identified with a Rapid Lipoproteomics Protocol

Abstract: Highlights d Rapid lipoproteomics assay in Mycobacterium smegmatis d Identifies L-arabinose ABC transporter substrate-binding protein MSMEG_1712 d L-arabinofuranose uptake via cognate ABC transporter MSMEG_1709-1711 d Crystal structure of MSMEG_1712 bound to L-arabinofuranose

Cited by 8 publications

References 81 publications

Transporters Involved in the Biogenesis and Functionalization of the Mycobacterial Cell Envelope

Transporters Involved in the Biogenesis and Functionalization of the Mycobacterial Cell Envelope

Asymmetric trehalose analogues to probe disaccharide processing pathways in mycobacteria

Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria

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