The TolC-like Protein HgdD of the Cyanobacterium Anabaena sp. PCC 7120 Is Involved in Secondary Metabolite Export and Antibiotic Resistance

Hahn, Alexander; Stevanovic, Mara; Mirus, Oliver; Schleiff, Enrico

doi:10.1074/jbc.m112.396010

Cited by 39 publications

(46 citation statements)

References 71 publications

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“…Although Anabaena sp. contains three open reading frames coding for distinct Omp85 proteins (17), the one encoded by alr2269 (hereafter referred to as anaOmp85) is considered the most abundant Omp85 protein in the outer membrane (18) and is the subject of this study. anaOmp85 contains three POTRA domains (anaP1, anaP2, and anaP3), which were found to regulate the pore gating of the b-barrel (5,15,19).…”

Section: Introductionmentioning

confidence: 99%

Relative Orientation of POTRA Domains from Cyanobacterial Omp85 Studied by Pulsed EPR Spectroscopy

Dastvan

Brouwer

Schuetz

et al. 2016

Biophysical Journal

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Many proteins of the outer membrane of Gram-negative bacteria and of the outer envelope of the endosymbiotically derived organelles mitochondria and plastids have a b-barrel fold. Their insertion is assisted by membrane proteins of the Omp85-TpsB superfamily. These proteins are composed of a C-terminal b-barrel and a different number of N-terminal POTRA domains, three in the case of cyanobacterial Omp85. Based on structural studies of Omp85 proteins, including the five POTRAdomain-containing BamA protein of Escherichia coli, it is predicted that anaP2 and anaP3 bear a fixed orientation, whereas anaP1 and anaP2 are connected via a flexible hinge. We challenged this proposal by investigating the conformational space of the N-terminal POTRA domains of Omp85 from the cyanobacterium Anabaena sp. PCC 7120 using pulsed electron-electron double resonance (PELDOR, or DEER) spectroscopy. The pronounced dipolar oscillations observed for most of the double spinlabeled positions indicate a rather rigid orientation of the POTRA domains in frozen liquid solution. Based on the PELDOR distance data, structure refinement of the POTRA domains was performed taking two different approaches: 1) treating the individual POTRA domains as rigid bodies; and 2) using an all-atom refinement of the structure. Both refinement approaches yielded ensembles of model structures that are more restricted compared to the conformational ensemble obtained by molecular dynamics simulations, with only a slightly different orientation of N-terminal POTRA domains anaP1 and anaP2 compared with the x-ray structure. The results are discussed in the context of the native environment of the POTRA domains in the periplasm.

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Section: Introductionmentioning

confidence: 99%

Relative Orientation of POTRA Domains from Cyanobacterial Omp85 Studied by Pulsed EPR Spectroscopy

Dastvan

Brouwer

Schuetz

et al. 2016

Biophysical Journal

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“…have been described previously (5,7,30). RNA was isolated from cells of a 25-ml culture at OD 750 ϭ 1.…”

Section: Methodsmentioning

confidence: 99%

“…Ethidium Uptake Measurement by DNA Intercalation-The Intercalation of ethidium into endogenous nucleic acids after uptake was monitored by the increase of fluorescence, as described previously (5). Data points were taken every minute for 30 min (excitation, 316 nm; emission, 620 nm (Tecan Infinite 200, CH)).…”

Section: )mentioning

confidence: 99%

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The Outer Membrane TolC-like Channel HgdD Is Part of Tripartite Resistance-Nodulation-Cell Division (RND) Efflux Systems Conferring Multiple-drug Resistance in the Cyanobacterium Anabaena sp. PCC7120

Hahn

Stevanovic

Mirus

et al. 2013

Journal of Biological Chemistry

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Two DevBCA‐like ABC transporters are involved in the multidrug resistance of the cyanobacterium Anabaena sp. PCC 7120

2019

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The filamentous heterocyst‐forming cyanobacterium Anabaena sp. PCC 7120 is an important model organism for studying cell differentiation, nitrogen fixation, and photosynthesis. This cyanobacterium possesses a high number of membrane transporters. Not much is known about the roles of the membrane transporters, especially the ATP‐binding cassette (ABC) transporters, in the multidrug resistance of this cyanobacterium. In the present work, we performed a mutational analysis of the genes alr4280/alr4281/alr4282 and alr3647/alr3648/alr3649 that code for the components of putative ABC exporters and are homologous to the DevBCA heterocyst‐specific glycolipid exporter. We show that these genes are essential for resistance to different drugs and are not essential for heterocyst development.

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The TolC-like Protein HgdD of the Cyanobacterium Anabaena sp. PCC 7120 Is Involved in Secondary Metabolite Export and Antibiotic Resistance

Cited by 39 publications

References 71 publications

Relative Orientation of POTRA Domains from Cyanobacterial Omp85 Studied by Pulsed EPR Spectroscopy

Relative Orientation of POTRA Domains from Cyanobacterial Omp85 Studied by Pulsed EPR Spectroscopy

The Outer Membrane TolC-like Channel HgdD Is Part of Tripartite Resistance-Nodulation-Cell Division (RND) Efflux Systems Conferring Multiple-drug Resistance in the Cyanobacterium Anabaena sp. PCC7120

Two DevBCA‐like ABC transporters are involved in the multidrug resistance of the cyanobacterium Anabaena sp. PCC 7120

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