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Article: An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli

TitleAn undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli
Authors
Issue Date2007
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2007, v. 282 n. 49, p. 36077-36089 How to Cite?
AbstractModification of lipid A with the 4-amino-4-deoxy-L-arabinose (L-Ara4N) moiety is required for resistance to polymyxin and cationic antimicrobial peptides in Escherichia coli and Salmonella typhimurium. An operon of seven genes (designated pmrHFIJKLM in S. typhimurium), which is regulated by the PmrA transcription factor and is also present in E. coli, is necessary for the maintenance of polymyxin resistance. We previously elucidated the roles of pmrHFIJK in the biosynthesis and attachment of L-Ara4N to lipid A and renamed these genes arn-BCADT, respectively. We now propose functions for the last two genes of the operon, pmrL and pmrM. Chromosomal inactivation of each of these genes in an E. coli pmrAc parent switched its phenotype from polymyxin-resistant to polymyxin-sensitive. Lipid A was no longer modified with L-Ara4N, even though the levels of the lipid-linked donor of the L-Ara4N moiety, undecaprenyl phosphate-α-L-Ara4N, were not reduced in the mutants. However, the undecaprenyl phosphate-α-L-Ara4N present in the mutants was less concentrated on the periplasmic surface of the inner membrane, as judged by 4-5-fold reduced labeling with the inner membrane-impermeable amine reagent N-hydroxysulfosuccinimidobiotin. In an arnT mutant of the same pmrAc parent, which lacks the enzyme that transfers the L-Ara4N unit to lipid A but retains the same high levels of undecaprenyl phosphate-α-L-Ara4N as the parent, N-hydroxysulfosuccinimidobiotin labeling was not reduced. These results implicate pmrL and pmrM, but not arnT, in transporting undecaprenyl phosphate-α-L-Ara4N across the inner membrane. PmrM and PmrL, now renamed ArnE and ArnF because of their involvement in L-Ara4N modification of lipid A, may be subunits of an undecaprenyl phosphate-α-L-Ara4N flippase. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/179028
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYan, Aen_US
dc.contributor.authorGuan, Zen_US
dc.contributor.authorRaetz, CRHen_US
dc.date.accessioned2012-12-19T09:51:32Z-
dc.date.available2012-12-19T09:51:32Z-
dc.date.issued2007en_US
dc.identifier.citationJournal Of Biological Chemistry, 2007, v. 282 n. 49, p. 36077-36089en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/179028-
dc.description.abstractModification of lipid A with the 4-amino-4-deoxy-L-arabinose (L-Ara4N) moiety is required for resistance to polymyxin and cationic antimicrobial peptides in Escherichia coli and Salmonella typhimurium. An operon of seven genes (designated pmrHFIJKLM in S. typhimurium), which is regulated by the PmrA transcription factor and is also present in E. coli, is necessary for the maintenance of polymyxin resistance. We previously elucidated the roles of pmrHFIJK in the biosynthesis and attachment of L-Ara4N to lipid A and renamed these genes arn-BCADT, respectively. We now propose functions for the last two genes of the operon, pmrL and pmrM. Chromosomal inactivation of each of these genes in an E. coli pmrAc parent switched its phenotype from polymyxin-resistant to polymyxin-sensitive. Lipid A was no longer modified with L-Ara4N, even though the levels of the lipid-linked donor of the L-Ara4N moiety, undecaprenyl phosphate-α-L-Ara4N, were not reduced in the mutants. However, the undecaprenyl phosphate-α-L-Ara4N present in the mutants was less concentrated on the periplasmic surface of the inner membrane, as judged by 4-5-fold reduced labeling with the inner membrane-impermeable amine reagent N-hydroxysulfosuccinimidobiotin. In an arnT mutant of the same pmrAc parent, which lacks the enzyme that transfers the L-Ara4N unit to lipid A but retains the same high levels of undecaprenyl phosphate-α-L-Ara4N as the parent, N-hydroxysulfosuccinimidobiotin labeling was not reduced. These results implicate pmrL and pmrM, but not arnT, in transporting undecaprenyl phosphate-α-L-Ara4N across the inner membrane. PmrM and PmrL, now renamed ArnE and ArnF because of their involvement in L-Ara4N modification of lipid A, may be subunits of an undecaprenyl phosphate-α-L-Ara4N flippase. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAmino Sugars - Genetics - Metabolismen_US
dc.subject.meshAnti-Bacterial Agents - Metabolism - Pharmacologyen_US
dc.subject.meshBacterial Proteins - Genetics - Metabolismen_US
dc.subject.meshBiological Transport - Physiologyen_US
dc.subject.meshCarboxy-Lyases - Genetics - Metabolismen_US
dc.subject.meshCarrier Proteins - Genetics - Metabolismen_US
dc.subject.meshCell Membrane - Genetics - Metabolismen_US
dc.subject.meshDrug Resistance, Bacterial - Physiologyen_US
dc.subject.meshEscherichia Coli - Genetics - Metabolismen_US
dc.subject.meshGene Silencingen_US
dc.subject.meshHexosyltransferases - Genetics - Metabolismen_US
dc.subject.meshLipid A - Genetics - Metabolismen_US
dc.subject.meshOperon - Physiologyen_US
dc.subject.meshPeriplasm - Genetics - Metabolismen_US
dc.subject.meshPolymyxins - Metabolism - Pharmacologyen_US
dc.subject.meshSalmonella Typhimurium - Genetics - Metabolismen_US
dc.titleAn undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia colien_US
dc.typeArticleen_US
dc.identifier.emailYan, A: ayan8@hku.hken_US
dc.identifier.authorityYan, A=rp00823en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.M706172200en_US
dc.identifier.pmid17928292-
dc.identifier.scopuseid_2-s2.0-37249025572en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-37249025572&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume282en_US
dc.identifier.issue49en_US
dc.identifier.spage36077en_US
dc.identifier.epage36089en_US
dc.identifier.eissn1083-351X-
dc.identifier.isiWOS:000251458100067-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridYan, A=8621667000en_US
dc.identifier.scopusauthoridGuan, Z=7202541986en_US
dc.identifier.scopusauthoridRaetz, CRH=7102514726en_US

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