TonB Interacts with Nonreceptor Proteins in the Outer Membrane of Escherichia coli

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Published in:	Journal of Bacteriology Vol. 184; no. 6; pp. 1640 - 1648
Main Authors:	Higgs, Penelope I, Letain, Tracy E, Merriam, Kelley K, Burke, Neal S, Park, HaJeung, Kang, ChulHee, Postle, Kathleen
Format:	Journal Article
Language:	English
Published:	United States American Society for Microbiology 01-03-2002
Subjects:	Bacteria Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins - metabolism Bacteriology Biological Transport Carrier Proteins - genetics Carrier Proteins - metabolism enterobactin enterochelin Escherichia coli Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism FepA protein Lipoproteins Lpp protein Membrane Proteins - metabolism Membranes Microbial Cell Biology murein Mutation OmpA protein Protein Binding Proteins Protons siderophores Sodium Chloride TonB protein
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Abstract	Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: JB
AbstractList	The Escherichia coli TonB protein serves to couple the cytoplsmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin B12 across the outer membrane. Consistent with this role, TonB has been demonstrated to prarticipate in strong interactions with bot hthe cytoplasmic and outer membranes. The Escherichia coli TonB protein serves to couple the cytoplasmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin B 12 across the outer membrane. Consistent with this role, TonB has been demonstrated to participate in strong interactions with both the cytoplasmic and outer membranes. The cytoplasmic membrane determinants for that interaction have been previously characterized in some detail. Here we begin to examine the nature of TonB interactions with the outer membrane. Although the presence of the siderophore enterochelin (also known as enterobactin) greatly enhanced detectable cross-linking between TonB and the outer membrane receptor, FepA, the absence of enterochelin did not prevent the localization of TonB to the outer membrane. Furthermore, the absence of FepA or indeed of all the iron-responsive outer membrane receptors did not alter this association of TonB with the outer membrane. This suggested that TonB interactions with the outer membrane were not limited to the TonB-dependent outer membrane receptors. Hydrolysis of the murein layer with lysozyme did not alter the distribution of TonB, suggesting that peptidoglycan was not responsible for the outer membrane association of TonB. Conversely, the interaction of TonB with the outer membrane was disrupted by the addition of 4 M NaCl, suggesting that these interactions were proteinaceous. Subsequently, two additional contacts of TonB with the outer membrane proteins Lpp and, putatively, OmpA were identified by in vivo cross-linking. These contacts corresponded to the 43-kDa and part of the 77-kDa TonB-specific complexes described previously. Surprisingly, mutations in these proteins individually did not appear to affect TonB phenotypes. These results suggest that there may be multiple redundant sites where TonB can interact with the outer membrane prior to transducing energy to the outer membrane receptors. The Escherichia coli TonB protein serves to couple the cytoplasmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin B sub(12) across the outer membrane. Consistent with this role, TonB has been demonstrated to participate in strong interactions with both the cytoplasmic and outer membranes. The cytoplasmic membrane determinants for that interaction have been previously characterized in some detail. Here we begin to examine the nature of TonB interactions with the outer membrane. Although the presence of the siderophore enterochelin (also known as enterobactin) greatly enhanced detectable cross-linking between TonB and the outer membrane receptor, FepA, the absence of enterochelin did not prevent the localization of TonB to the outer membrane. Furthermore, the absence of FepA or indeed of all the iron- responsive outer membrane receptors did not alter this association of TonB with the outer membrane. This suggested that TonB interactions with the outer membrane were not limited to the TonB-dependent outer membrane receptors. Hydrolysis of the murein layer with lysozyme did not alter the distribution of TonB, suggesting that peptidoglycan was not responsible for the outer membrane association of TonB. Conversely, the interaction of TonB with the outer membrane was disrupted by the addition of 4 M NaCl, suggesting that these interactions were proteinaceous. Subsequently, two additional contacts of TonB with the outer membrane proteins Lpp and, putatively, OmpA were identified by in vivo cross- linking. These contacts corresponded to the 43-kDa and part of the 77-kDa TonB- specific complexes described previously. Surprisingly, mutations in these proteins individually did not appear to affect TonB phenotypes. These results suggest that there may be multiple redundant sites where TonB can interact with the outer membrane prior to transducing energy to the outer membrane receptors. Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: JB The Escherichia coli TonB protein serves to couple the cytoplasmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin B(12) across the outer membrane. Consistent with this role, TonB has been demonstrated to participate in strong interactions with both the cytoplasmic and outer membranes. The cytoplasmic membrane determinants for that interaction have been previously characterized in some detail. Here we begin to examine the nature of TonB interactions with the outer membrane. Although the presence of the siderophore enterochelin (also known as enterobactin) greatly enhanced detectable cross-linking between TonB and the outer membrane receptor, FepA, the absence of enterochelin did not prevent the localization of TonB to the outer membrane. Furthermore, the absence of FepA or indeed of all the iron-responsive outer membrane receptors did not alter this association of TonB with the outer membrane. This suggested that TonB interactions with the outer membrane were not limited to the TonB-dependent outer membrane receptors. Hydrolysis of the murein layer with lysozyme did not alter the distribution of TonB, suggesting that peptidoglycan was not responsible for the outer membrane association of TonB. Conversely, the interaction of TonB with the outer membrane was disrupted by the addition of 4 M NaCl, suggesting that these interactions were proteinaceous. Subsequently, two additional contacts of TonB with the outer membrane proteins Lpp and, putatively, OmpA were identified by in vivo cross-linking. These contacts corresponded to the 43-kDa and part of the 77-kDa TonB-specific complexes described previously. Surprisingly, mutations in these proteins individually did not appear to affect TonB phenotypes. These results suggest that there may be multiple redundant sites where TonB can interact with the outer membrane prior to transducing energy to the outer membrane receptors.The Escherichia coli TonB protein serves to couple the cytoplasmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin B(12) across the outer membrane. Consistent with this role, TonB has been demonstrated to participate in strong interactions with both the cytoplasmic and outer membranes. The cytoplasmic membrane determinants for that interaction have been previously characterized in some detail. Here we begin to examine the nature of TonB interactions with the outer membrane. Although the presence of the siderophore enterochelin (also known as enterobactin) greatly enhanced detectable cross-linking between TonB and the outer membrane receptor, FepA, the absence of enterochelin did not prevent the localization of TonB to the outer membrane. Furthermore, the absence of FepA or indeed of all the iron-responsive outer membrane receptors did not alter this association of TonB with the outer membrane. This suggested that TonB interactions with the outer membrane were not limited to the TonB-dependent outer membrane receptors. Hydrolysis of the murein layer with lysozyme did not alter the distribution of TonB, suggesting that peptidoglycan was not responsible for the outer membrane association of TonB. Conversely, the interaction of TonB with the outer membrane was disrupted by the addition of 4 M NaCl, suggesting that these interactions were proteinaceous. Subsequently, two additional contacts of TonB with the outer membrane proteins Lpp and, putatively, OmpA were identified by in vivo cross-linking. These contacts corresponded to the 43-kDa and part of the 77-kDa TonB-specific complexes described previously. Surprisingly, mutations in these proteins individually did not appear to affect TonB phenotypes. These results suggest that there may be multiple redundant sites where TonB can interact with the outer membrane prior to transducing energy to the outer membrane receptors. The Escherichia coli TonB protein serves to couple the cytoplasmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin B(12) across the outer membrane. Consistent with this role, TonB has been demonstrated to participate in strong interactions with both the cytoplasmic and outer membranes. The cytoplasmic membrane determinants for that interaction have been previously characterized in some detail. Here we begin to examine the nature of TonB interactions with the outer membrane. Although the presence of the siderophore enterochelin (also known as enterobactin) greatly enhanced detectable cross-linking between TonB and the outer membrane receptor, FepA, the absence of enterochelin did not prevent the localization of TonB to the outer membrane. Furthermore, the absence of FepA or indeed of all the iron-responsive outer membrane receptors did not alter this association of TonB with the outer membrane. This suggested that TonB interactions with the outer membrane were not limited to the TonB-dependent outer membrane receptors. Hydrolysis of the murein layer with lysozyme did not alter the distribution of TonB, suggesting that peptidoglycan was not responsible for the outer membrane association of TonB. Conversely, the interaction of TonB with the outer membrane was disrupted by the addition of 4 M NaCl, suggesting that these interactions were proteinaceous. Subsequently, two additional contacts of TonB with the outer membrane proteins Lpp and, putatively, OmpA were identified by in vivo cross-linking. These contacts corresponded to the 43-kDa and part of the 77-kDa TonB-specific complexes described previously. Surprisingly, mutations in these proteins individually did not appear to affect TonB phenotypes. These results suggest that there may be multiple redundant sites where TonB can interact with the outer membrane prior to transducing energy to the outer membrane receptors.
Author	Kathleen Postle ChulHee Kang Neal S. Burke Penelope I. Higgs HaJeung Park Tracy E. Letain Kelley K. Merriam
AuthorAffiliation	School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4233
AuthorAffiliation_xml	– name: School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4233
Author_xml	– sequence: 1 givenname: Penelope I surname: Higgs fullname: Higgs, Penelope I organization: School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4233, USA – sequence: 2 givenname: Tracy E surname: Letain fullname: Letain, Tracy E – sequence: 3 givenname: Kelley K surname: Merriam fullname: Merriam, Kelley K – sequence: 4 givenname: Neal S surname: Burke fullname: Burke, Neal S – sequence: 5 givenname: HaJeung surname: Park fullname: Park, HaJeung – sequence: 6 givenname: ChulHee surname: Kang fullname: Kang, ChulHee – sequence: 7 givenname: Kathleen surname: Postle fullname: Postle, Kathleen
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Cites_doi	10.1016/S0021-9258(18)38069-4 10.1128/jb.136.1.280-285.1978 10.1128/jb.171.9.5127-5134.1989 10.1128/jb.106.1.51-57.1971 10.1007/BF00328074 10.1128/JB.183.9.2755-2764.2001 10.1128/jb.171.8.4442-4447.1989 10.1016/S0968-0004(99)01359-6 10.1128/JB.180.22.6031-6038.1998 10.1016/S0021-9258(20)81822-5 10.1074/jbc.M007479200 10.1111/j.1365-2958.1990.tb00562.x 10.1128/AAC.32.12.1879 10.1111/j.1574-6968.1999.tb13731.x 10.1074/jbc.272.45.28391 10.1046/j.1365-2958.2000.02190.x 10.1128/jb.165.1.107-115.1986 10.1016/S0021-9258(19)85421-2 10.1111/j.1365-2958.1993.tb00966.x 10.1111/j.1365-2958.1993.tb01570.x 10.1073/pnas.80.17.5235 10.1046/j.1365-2958.1999.01317.x 10.1128/jb.169.6.2667-2674.1987 10.1139/m79-065 10.1007/BF00770246 10.1016/0005-2787(76)90231-8 10.1128/jb.176.8.2326-2338.1994 10.1128/jb.178.14.4031-4038.1996 10.1046/j.1365-2958.1998.00945.x 10.1073/pnas.74.4.1417 10.1128/JB.183.22.6538-6542.2001 10.1074/jbc.M102778200 10.1128/jb.119.3.726-735.1974 10.1128/jb.178.5.1363-1373.1996 10.1016/0304-4165(67)90106-7 10.1128/JB.180.18.4872-4878.1998 10.1016/0304-4157(75)90013-1 10.1016/S1369-5274(98)80017-9 10.1046/j.1365-2958.1997.3331703.x 10.1128/jb.161.3.1219-1221.1985 10.1073/pnas.78.11.7069 10.1046/j.1365-2958.1998.00817.x 10.1016/0003-2697(87)90612-9 10.1111/j.1365-2958.1994.tb00457.x 10.1128/mr.53.1.1-24.1989
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Notes	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Present address: Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, ID 83844. Corresponding author. Mailing address: School of Molecular Biosciences, Washington State University, Pullman, WA 99164-4233. Phone: (509) 335-5614. Fax: (509) 335-1907. E-mail: postle@mail.wsu.edu. Present address: Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720. Present address: Lawrence Berkeley National Laboratory, Earth Science Division, Berkeley, CA 94720.
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References	e_1_3_2_28_2 (e_1_3_2_7_2) 2001; 276 (e_1_3_2_27_2) 1997; 24 (e_1_3_2_35_2) 1987; 160 (e_1_3_2_4_2) 1993; 8 e_1_3_2_41_2 e_1_3_2_40_2 (e_1_3_2_32_2) 1993; 25 e_1_3_2_43_2 e_1_3_2_21_2 e_1_3_2_42_2 (e_1_3_2_20_2) 1998; 1 (e_1_3_2_37_2) 1993; 268 e_1_3_2_45_2 (e_1_3_2_15_2) 1981; 78 e_1_3_2_44_2 e_1_3_2_47_2 (e_1_3_2_23_2) 1999; 31 (e_1_3_2_30_2) 1997; 272 (e_1_3_2_12_2) 1976; 454 (e_1_3_2_24_2) 1994; 13 (e_1_3_2_46_2) 1967; 141 (e_1_3_2_26_2) 1999; 177 (e_1_3_2_17_2) 1972; 247 (e_1_3_2_33_2) 1983; 80 (e_1_3_2_29_2) 1998; 28 (e_1_3_2_25_2) 1993; 10 e_1_3_2_9_2 e_1_3_2_38_2 e_1_3_2_18_2 e_1_3_2_39_2 (e_1_3_2_19_2) 1990; 4 (e_1_3_2_3_2) 1975; 415 (e_1_3_2_11_2) 1979; 25 e_1_3_2_10_2 (e_1_3_2_13_2) 1984; 196 e_1_3_2_31_2 (e_1_3_2_34_2) 1988; 263 e_1_3_2_36_2 e_1_3_2_2_2 e_1_3_2_14_2 (e_1_3_2_5_2) 1999; 24 (e_1_3_2_16_2) 1977; 74 (e_1_3_2_6_2) 2000; 38 (e_1_3_2_22_2) 2001; 276 (e_1_3_2_8_2) 1998; 29
References_xml	– volume: 263 start-page: 11000 year: 1988 ident: e_1_3_2_34_2 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)38069-4 – ident: e_1_3_2_40_2 doi: 10.1128/jb.136.1.280-285.1978 – ident: e_1_3_2_10_2 doi: 10.1128/jb.171.9.5127-5134.1989 – ident: e_1_3_2_47_2 doi: 10.1128/jb.106.1.51-57.1971 – volume: 196 start-page: 367 year: 1984 ident: e_1_3_2_13_2 publication-title: Mol. Gen. Genet. doi: 10.1007/BF00328074 – ident: e_1_3_2_31_2 doi: 10.1128/JB.183.9.2755-2764.2001 – ident: e_1_3_2_38_2 doi: 10.1128/jb.171.8.4442-4447.1989 – volume: 24 start-page: 104 year: 1999 ident: e_1_3_2_5_2 publication-title: Trends Biochem. Sci. doi: 10.1016/S0968-0004(99)01359-6 – ident: e_1_3_2_14_2 doi: 10.1128/JB.180.22.6031-6038.1998 – volume: 247 start-page: 8154 year: 1972 ident: e_1_3_2_17_2 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(20)81822-5 – volume: 276 start-page: 8111 year: 2001 ident: e_1_3_2_22_2 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M007479200 – volume: 4 start-page: 2027 year: 1990 ident: e_1_3_2_19_2 publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1990.tb00562.x – ident: e_1_3_2_9_2 doi: 10.1128/AAC.32.12.1879 – volume: 177 start-page: 191 year: 1999 ident: e_1_3_2_26_2 publication-title: FEMS Microbiol. Lett. doi: 10.1111/j.1574-6968.1999.tb13731.x – volume: 272 start-page: 28391 year: 1997 ident: e_1_3_2_30_2 publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.45.28391 – volume: 38 start-page: 904 year: 2000 ident: e_1_3_2_6_2 publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2000.02190.x – ident: e_1_3_2_41_2 doi: 10.1128/jb.165.1.107-115.1986 – volume: 268 start-page: 16302 year: 1993 ident: e_1_3_2_37_2 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)85421-2 – volume: 10 start-page: 943 year: 1993 ident: e_1_3_2_25_2 publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1993.tb00966.x – volume: 8 start-page: 261 year: 1993 ident: e_1_3_2_4_2 publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1993.tb01570.x – volume: 80 start-page: 5235 year: 1983 ident: e_1_3_2_33_2 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.80.17.5235 – volume: 31 start-page: 1809 year: 1999 ident: e_1_3_2_23_2 publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.1999.01317.x – ident: e_1_3_2_42_2 doi: 10.1128/jb.169.6.2667-2674.1987 – volume: 25 start-page: 423 year: 1979 ident: e_1_3_2_11_2 publication-title: Can. J. Microbiol. doi: 10.1139/m79-065 – ident: e_1_3_2_28_2 – volume: 25 start-page: 591 year: 1993 ident: e_1_3_2_32_2 publication-title: J. Bioenerg. Biomembr. doi: 10.1007/BF00770246 – volume: 454 start-page: 285 year: 1976 ident: e_1_3_2_12_2 publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2787(76)90231-8 – ident: e_1_3_2_18_2 doi: 10.1128/jb.176.8.2326-2338.1994 – ident: e_1_3_2_44_2 doi: 10.1128/jb.178.14.4031-4038.1996 – volume: 29 start-page: 359 year: 1998 ident: e_1_3_2_8_2 publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.1998.00945.x – volume: 74 start-page: 1417 year: 1977 ident: e_1_3_2_16_2 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.74.4.1417 – ident: e_1_3_2_43_2 doi: 10.1128/JB.183.22.6538-6542.2001 – volume: 276 start-page: 27535 year: 2001 ident: e_1_3_2_7_2 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M102778200 – ident: e_1_3_2_39_2 doi: 10.1128/jb.119.3.726-735.1974 – ident: e_1_3_2_21_2 doi: 10.1128/jb.178.5.1363-1373.1996 – volume: 141 start-page: 319 year: 1967 ident: e_1_3_2_46_2 publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4165(67)90106-7 – ident: e_1_3_2_2_2 doi: 10.1128/JB.180.18.4872-4878.1998 – volume: 415 start-page: 335 year: 1975 ident: e_1_3_2_3_2 publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4157(75)90013-1 – volume: 1 start-page: 238 year: 1998 ident: e_1_3_2_20_2 publication-title: Curr. Opin. Microbiol. doi: 10.1016/S1369-5274(98)80017-9 – volume: 24 start-page: 271 year: 1997 ident: e_1_3_2_27_2 publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.1997.3331703.x – ident: e_1_3_2_45_2 doi: 10.1128/jb.161.3.1219-1221.1985 – volume: 78 start-page: 7069 year: 1981 ident: e_1_3_2_15_2 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.78.11.7069 – volume: 28 start-page: 675 year: 1998 ident: e_1_3_2_29_2 publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.1998.00817.x – volume: 160 start-page: 47 year: 1987 ident: e_1_3_2_35_2 publication-title: Anal. Biochem. doi: 10.1016/0003-2697(87)90612-9 – volume: 13 start-page: 627 year: 1994 ident: e_1_3_2_24_2 publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1994.tb00457.x – ident: e_1_3_2_36_2 doi: 10.1128/mr.53.1.1-24.1989
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Snippet	Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... The Escherichia coli TonB protein serves to couple the cytoplasmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin... The Escherichia coli TonB protein serves to couple the cytoplasmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin B... The Escherichia coli TonB protein serves to couple the cytoplsmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin... The Escherichia coli TonB protein serves to couple the cytoplasmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin B...
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SubjectTerms	Bacteria Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins - metabolism Bacteriology Biological Transport Carrier Proteins - genetics Carrier Proteins - metabolism enterobactin enterochelin Escherichia coli Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism FepA protein Lipoproteins Lpp protein Membrane Proteins - metabolism Membranes Microbial Cell Biology murein Mutation OmpA protein Protein Binding Proteins Protons siderophores Sodium Chloride TonB protein
Title	TonB Interacts with Nonreceptor Proteins in the Outer Membrane of Escherichia coli
URI	http://jb.asm.org/content/184/6/1640.abstract https://www.ncbi.nlm.nih.gov/pubmed/11872715 https://www.proquest.com/docview/227104118 https://search.proquest.com/docview/18282538 https://www.proquest.com/docview/71487505 https://pubmed.ncbi.nlm.nih.gov/PMC134908
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