Roles of the Protruding Loop of Factor B Essential for the Localization of Lipoproteins (LolB) in the Anchoring of Bacterial Triacylated Proteins to the Outer Membrane

Hayashi, Yoshie; Tsurumizu, Ryoji; Tsukahara, Jun; Takeda, Kazuki; Narita, Shin‐ichiro; Mori, Makiko; Miki, Kunio; Tokuda, Harukuni

doi:10.1074/jbc.m113.539270

Cited by 24 publications

(29 citation statements)

References 25 publications

(39 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Transfer of lipoprotein from LolA to LolB occurs spontaneously, indicating that the transfer is affinity-driven (26). Finally, LolB inserts the lipoprotein via its acyl tails into the inner leaflet of the OM (27, ASBMB AWARD ARTICLE: Intermembrane lipid trafficking in bacteria 28); the mechanism for this step is not known but is also energy-independent, consistent with the idea that the triacyl moiety anchored in the membrane would be the most stable state (Fig. 2).…”

Section: Lipoprotein Traffickingsupporting

confidence: 60%

Lipid trafficking across the Gram-negative cell envelope

Shrivastava

Chng

2019

Journal of Biological Chemistry

View full text Add to dashboard Cite

Edited by Karen G. Fleming The outer membrane (OM) of Gram-negative bacteria exhibits unique lipid asymmetry, with lipopolysaccharides (LPS) residing in the outer leaflet and phospholipids (PLs) in the inner leaflet. This asymmetric bilayer protects the bacterium against intrusion of many toxic substances, including antibiotics and detergents, yet allows acquisition of nutrients necessary for growth. To build the OM and ensure its proper function, the cell produces OM constituents in the cytoplasm or inner membrane and transports these components across the aqueous periplasmic space separating the two membranes. Of note, the processes by which the most basic membrane building blocks, i.e. PLs, are shuttled across the cell envelope remain elusive. This review highlights our current understanding (or lack thereof) of bacterial PL trafficking, with a focus on recent developments in the field. We adopt a mechanistic approach and draw parallels and comparisons with well-characterized systems, particularly OM lipoprotein and LPS transport, to illustrate key challenges in intermembrane lipid trafficking. Pathways that transport PLs across the bacterial cell envelope are fundamental to OM biogenesis and homeostasis and are potential molecular targets that could be exploited for antibiotic development.

show abstract

Section: Lipoprotein Traffickingsupporting

confidence: 60%

Lipid trafficking across the Gram-negative cell envelope

Shrivastava

Chng

2019

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…While non-OM proteins were on average up-regulated in the absence of Ara by 16% (median increase of 2 0.22 = 1.16), OM proteins were on average down-regulated by 21% (median decrease of 2 À0.33 = 0.79) (Figure 2A). Of interest were LolB and OmpA, responsible for stable anchoring of drug-efflux pumps to the OM (Hayashi et al, 2014;Tsukahara et al, 2009) and for anchoring the OM to the peptidoglycan cell wall, respectively. lolB and ompA are enriched with Pro codons relative to the average codon usage in E. coli protein-coding genes ( Figure 2B, lolB: CCN [6.7% versus 4.3%] and CC[C/U] [2.4% versus 1.1%]) and ompA CCN [5.5% versus 4.3%]).…”

Section: Results M 1 G37-deficient E Coli and Salmonella Have Lower mentioning

confidence: 99%

tRNA Methylation Is a Global Determinant of Bacterial Multi-drug Resistance

et al. 2019

View full text Add to dashboard Cite

Bacterial multi‐drug resistance is a burgeoning crisis whose origin remains mechanistically opaque. Through altered permeability or efflux activity, the membrane prevents many antibiotics from reaching high enough intracellular concentrations to exert a therapeutic effect. We show here that protein synthesis of membrane‐associated genes involves translation of proline CC[C/U] codons, which require N1‐methylation of guanosine 37 (m1G37) on the 3′‐side of the tRNA anticodon. TrmD is the bacterial methyl transferase that catalyzes m1G37‐methylation. Removal of m1G37 by trmD inactivation reduces biosynthesis of membrane proteins, impairs membrane structure and mechanics, and sensitizes Gram‐negative bacteria to multiple classes of antibiotics and suppresses development of resistance and persistence. Codon engineering in the major efflux gene tolC removes the dependence on trmD for biosynthesis of membrane proteins. TrmD activity requires the conserved G37 in tRNAPro; replacement of G37 with C37 increases membrane permeability and accelerates cell death. These findings demonstrate the potential to diminish multi‐drug resistance by inaction of TrmD and its m1G37‐tRNA product. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.

show abstract

“…A loop that protrudes from the core LolB structure is important for the insertion reaction. Mutation of Leu within this loop yields LolB variants that can receive lipoproteins from LolA but then fail to insert them . To insert lipoproteins, LolB must somehow disrupt the OM bilayer organization to facilitate acyl chain insertion.…”

Section: Crossing the Great Periplasmic Divide And Onwards To The Ommentioning

confidence: 99%

Lipoprotein Transport: Greasing the Machines of Outer Membrane Biogenesis

Grabowicz

2018

BioEssays

View full text Add to dashboard Cite

The Gram-negative outer membrane (OM) is a potent permeability barrier against antibiotics, limiting clinical options amid mounting rates of resistance. The Lol transport pathway delivers lipoproteins to the OM. All the OM assembly machines require one or more OM lipoprotein to function, making the Lol pathway central for all aspects of OM biogenesis. The Lol pathways of many medically important species clearly deviate from the Escherichia coli paradigm, perhaps with implications for efforts to develop novel antibiotics. Moreover, recent work reveals the existence of an undiscovered alternate route for bringing lipoproteins to the OM. Here, lipoprotein transport mechanisms, and the quality control systems that underpin them, is re-examined in context of their diversity.

show abstract

Roles of the Protruding Loop of Factor B Essential for the Localization of Lipoproteins (LolB) in the Anchoring of Bacterial Triacylated Proteins to the Outer Membrane

Cited by 24 publications

References 25 publications

Lipid trafficking across the Gram-negative cell envelope

Lipid trafficking across the Gram-negative cell envelope

tRNA Methylation Is a Global Determinant of Bacterial Multi-drug Resistance

Lipoprotein Transport: Greasing the Machines of Outer Membrane Biogenesis

Contact Info

Product

Resources

About