Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein
The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB a...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Prinz, Thorsten [verfasserIn] Tommassen, Jan [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 2000 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: FEMS microbiology letters - Federation of European Microbiological Societies ; GKD-ID: 114439X, Oxford [u.a.] : Wiley-Blackwell, 1977, 183(2000), 1, Seite 0 |
| Übergeordnetes Werk: |
volume:183 ; year:2000 ; number:1 ; pages:0 |
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| DOI / URN: |
10.1111/j.1574-6968.2000.tb08932.x |
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| 520 | |a The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins. | ||
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10.1111/j.1574-6968.2000.tb08932.x doi (DE-627)NLEJ242901654 DE-627 ger DE-627 rakwb Prinz, Thorsten verfasserin aut Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein Oxford, UK Blackwell Publishing Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| RmpM protein Tommassen, Jan verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 183(2000), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:183 year:2000 number:1 pages:0 http://dx.doi.org/10.1111/j.1574-6968.2000.tb08932.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 183 2000 1 0 |
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10.1111/j.1574-6968.2000.tb08932.x doi (DE-627)NLEJ242901654 DE-627 ger DE-627 rakwb Prinz, Thorsten verfasserin aut Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein Oxford, UK Blackwell Publishing Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| RmpM protein Tommassen, Jan verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 183(2000), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:183 year:2000 number:1 pages:0 http://dx.doi.org/10.1111/j.1574-6968.2000.tb08932.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 183 2000 1 0 |
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10.1111/j.1574-6968.2000.tb08932.x doi (DE-627)NLEJ242901654 DE-627 ger DE-627 rakwb Prinz, Thorsten verfasserin aut Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein Oxford, UK Blackwell Publishing Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| RmpM protein Tommassen, Jan verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 183(2000), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:183 year:2000 number:1 pages:0 http://dx.doi.org/10.1111/j.1574-6968.2000.tb08932.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 183 2000 1 0 |
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10.1111/j.1574-6968.2000.tb08932.x doi (DE-627)NLEJ242901654 DE-627 ger DE-627 rakwb Prinz, Thorsten verfasserin aut Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein Oxford, UK Blackwell Publishing Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| RmpM protein Tommassen, Jan verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 183(2000), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:183 year:2000 number:1 pages:0 http://dx.doi.org/10.1111/j.1574-6968.2000.tb08932.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 183 2000 1 0 |
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10.1111/j.1574-6968.2000.tb08932.x doi (DE-627)NLEJ242901654 DE-627 ger DE-627 rakwb Prinz, Thorsten verfasserin aut Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein Oxford, UK Blackwell Publishing Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| RmpM protein Tommassen, Jan verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 183(2000), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:183 year:2000 number:1 pages:0 http://dx.doi.org/10.1111/j.1574-6968.2000.tb08932.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 183 2000 1 0 |
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Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein RmpM protein |
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Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein |
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The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins. |
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The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins. |
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The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ242901654</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707165728.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s2000 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1574-6968.2000.tb08932.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ242901654</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Prinz, Thorsten</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Association of iron-regulated outer membrane proteins of Neisseria meningitidis with the RmpM (class 4) protein</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">2000</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">RmpM protein</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Tommassen, Jan</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="a">Federation of European Microbiological Societies ; GKD-ID: 114439X</subfield><subfield code="t">FEMS microbiology letters</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1977</subfield><subfield code="g">183(2000), 1, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927053</subfield><subfield code="w">(DE-600)1501716-3</subfield><subfield code="x">1574-6968</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:183</subfield><subfield code="g">year:2000</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1574-6968.2000.tb08932.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">183</subfield><subfield code="j">2000</subfield><subfield code="e">1</subfield><subfield code="h">0</subfield></datafield></record></collection>
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