» Articles » PMID: 30307391

The Apolipoprotein N-acyl Transferase Lnt is Dispensable for Growth in Acinetobacter Species

Overview
Specialty Microbiology
Date 2018 Oct 12
PMID 30307391
Citations 11
Authors
Affiliations
Soon will be listed here.
Abstract

Directing the flow of protein traffic is a critical task faced by all cellular organisms. In Gram-negative bacteria, this traffic includes lipoproteins. Lipoproteins are synthesized as precursors in the cytoplasm and receive their acyl modifications upon export across the inner membrane. The third and final acyl chain is added by Lnt, which until recently was thought to be essential in all Gram-negatives. In this report, we show that Acinetobacter species can also tolerate a complete loss-of-function mutation in lnt. Absence of a fully functional Lnt impairs modification of lipoproteins, increases outer membrane permeability and susceptibility to antibiotics, and alters normal cellular morphology. In addition, we show that loss of lnt triggers a global transcriptional response to this added cellular stress. Taken together, our findings provide new insights on and support the growing revisions to the Gram-negative lipoprotein biogenesis paradigm.

Citing Articles

Outer membrane lipoproteins: late to the party, but the center of attention.

May K, Grabowicz M J Bacteriol. 2024; 207(1):e0044224.

PMID: 39670753 PMC: 11784454. DOI: 10.1128/jb.00442-24.


The BfmRS stress response protects against defects in outer membrane lipoprotein biogenesis.

Marotta J, Zhao A, Rather P, Grabowicz M J Bacteriol. 2024; 207(1):e0033224.

PMID: 39660887 PMC: 11784087. DOI: 10.1128/jb.00332-24.


Identification of determinants that allow maintenance of high-level fluoroquinolone resistance in .

Hamami E, Huo W, Hernandez-Bird J, Castaneda A, Bai J, Syal S mBio. 2024; 16(1):e0322124.

PMID: 39589129 PMC: 11708032. DOI: 10.1128/mbio.03221-24.


Identification and characterization of the lipoprotein -acyltransferase in .

Armbruster K, Jiang J, Sartorio M, Scott N, Peterson J, Sexton J Proc Natl Acad Sci U S A. 2024; 121(46):e2410909121.

PMID: 39495918 PMC: 11573676. DOI: 10.1073/pnas.2410909121.


Identification and Characterization of the Lipoprotein -acyltransferase in .

Armbruster K, Jiang J, Sartorio M, Scott N, Peterson J, Sexton J bioRxiv. 2024; .

PMID: 38853980 PMC: 11160734. DOI: 10.1101/2024.05.31.596883.


References
1.
Narita S, Tokuda H . Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins. J Biol Chem. 2007; 282(18):13372-8. DOI: 10.1074/jbc.M611839200. View

2.
Okuda S, Tokuda H . Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB. Proc Natl Acad Sci U S A. 2009; 106(14):5877-82. PMC: 2667047. DOI: 10.1073/pnas.0900896106. View

3.
Barchinger S, Ades S . Regulated proteolysis: control of the Escherichia coli σ(E)-dependent cell envelope stress response. Subcell Biochem. 2013; 66:129-60. DOI: 10.1007/978-94-007-5940-4_6. View

4.
HsuChen C, Feingold D . The mechanism of polymyxin B action and selectivity toward biologic membranes. Biochemistry. 1973; 12(11):2105-11. DOI: 10.1021/bi00735a014. View

5.
Murin C, Segal K, Bryksin A, Matsumura I . Expression vectors for Acinetobacter baylyi ADP1. Appl Environ Microbiol. 2011; 78(1):280-3. PMC: 3255645. DOI: 10.1128/AEM.05597-11. View