The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity
Structural information defining an N-terminal sequence required for the membrane sorting of bacterial lipoproteins has been previously garnered through the study of a hybrid outer membrane (OM) lipo-beta-lactamase (LL) (Ghrayeb and Inouye (1984) J. Biol. Chem. 259, 463-467). Introduction of an aspar...
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| Veröffentlicht in: | The Journal of biological chemistry 1991-09, Vol.266 (25), p.16458-16464 |
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| creator | GENNITY, J. M INOUYE, M |
| description | Structural information defining an N-terminal sequence required for the membrane sorting of bacterial lipoproteins has been
previously garnered through the study of a hybrid outer membrane (OM) lipo-beta-lactamase (LL) (Ghrayeb and Inouye (1984)
J. Biol. Chem. 259, 463-467). Introduction of an aspartate as the second residue of mature LL (D2 mutant) causes an inner
membrane (IM) localization of this protein (Yamaguchi, K., Yu, F., and Inouye, M. (1988) Cell 53, 423-432). Introduction of
as aspartate at the third residue of mature LL (D3) causes a weaker IM sorting signal and when present as the fourth residue
(D4), normal OM sorting occurs. A positively charged residue at the second position (K2) has no effect on OM localization.
Remarkably, glutamate substitution at either the second (E2) or third (E3) position does not interfere with OM sorting. Sorting
of the mutant D2 LL can be partially suppressed by introduction of a positively charged histidine (D2H3) or lysine (D2K3)
at residue 3 of the mature protein. These results indicate that both the negative charge of the aspartate residue and some
structural feature not present in a glutamate residue are required for sorting to the IM. The suppression of IM localization
of the D2H3 LL double mutant can be eliminated by growing Escherichia coli at pH 8.4 to reduce the histidine partial positive
charge. This result supports the essentiality of a negative charge in IM localization and indicates that the committed step
in lipoprotein sorting is made in a cellular compartment, the periplasm, at equilibrium with the external pH. |
| doi_str_mv | 10.1016/s0021-9258(18)55322-9 |
| format | Article |
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previously garnered through the study of a hybrid outer membrane (OM) lipo-beta-lactamase (LL) (Ghrayeb and Inouye (1984)
J. Biol. Chem. 259, 463-467). Introduction of an aspartate as the second residue of mature LL (D2 mutant) causes an inner
membrane (IM) localization of this protein (Yamaguchi, K., Yu, F., and Inouye, M. (1988) Cell 53, 423-432). Introduction of
as aspartate at the third residue of mature LL (D3) causes a weaker IM sorting signal and when present as the fourth residue
(D4), normal OM sorting occurs. A positively charged residue at the second position (K2) has no effect on OM localization.
Remarkably, glutamate substitution at either the second (E2) or third (E3) position does not interfere with OM sorting. Sorting
of the mutant D2 LL can be partially suppressed by introduction of a positively charged histidine (D2H3) or lysine (D2K3)
at residue 3 of the mature protein. These results indicate that both the negative charge of the aspartate residue and some
structural feature not present in a glutamate residue are required for sorting to the IM. The suppression of IM localization
of the D2H3 LL double mutant can be eliminated by growing Escherichia coli at pH 8.4 to reduce the histidine partial positive
charge. This result supports the essentiality of a negative charge in IM localization and indicates that the committed step
in lipoprotein sorting is made in a cellular compartment, the periplasm, at equilibrium with the external pH.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(18)55322-9</identifier><identifier>PMID: 1885579</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Bacterial Outer Membrane Proteins - metabolism ; Base Sequence ; beta-Lactamases - genetics ; beta-Lactamases - metabolism ; Biological and medical sciences ; DNA, Bacterial ; Electrochemistry ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli - genetics ; Escherichia coli - growth & development ; Escherichia coli - metabolism ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Lipoproteins - genetics ; Lipoproteins - metabolism ; Lipoproteins, myelin ; membrane proteins ; Molecular Sequence Data ; Mutagenesis ; mutants ; periplasmic space ; Proteins ; Suppression, Genetic</subject><ispartof>The Journal of biological chemistry, 1991-09, Vol.266 (25), p.16458-16464</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-2f2e4a409cebba6bc7faa78220a25c866415bb1bedd15530a83448928a369eb53</citedby><cites>FETCH-LOGICAL-c506t-2f2e4a409cebba6bc7faa78220a25c866415bb1bedd15530a83448928a369eb53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4991523$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1885579$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>GENNITY, J. M</creatorcontrib><creatorcontrib>INOUYE, M</creatorcontrib><title>The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Structural information defining an N-terminal sequence required for the membrane sorting of bacterial lipoproteins has been
previously garnered through the study of a hybrid outer membrane (OM) lipo-beta-lactamase (LL) (Ghrayeb and Inouye (1984)
J. Biol. Chem. 259, 463-467). Introduction of an aspartate as the second residue of mature LL (D2 mutant) causes an inner
membrane (IM) localization of this protein (Yamaguchi, K., Yu, F., and Inouye, M. (1988) Cell 53, 423-432). Introduction of
as aspartate at the third residue of mature LL (D3) causes a weaker IM sorting signal and when present as the fourth residue
(D4), normal OM sorting occurs. A positively charged residue at the second position (K2) has no effect on OM localization.
Remarkably, glutamate substitution at either the second (E2) or third (E3) position does not interfere with OM sorting. Sorting
of the mutant D2 LL can be partially suppressed by introduction of a positively charged histidine (D2H3) or lysine (D2K3)
at residue 3 of the mature protein. These results indicate that both the negative charge of the aspartate residue and some
structural feature not present in a glutamate residue are required for sorting to the IM. The suppression of IM localization
of the D2H3 LL double mutant can be eliminated by growing Escherichia coli at pH 8.4 to reduce the histidine partial positive
charge. This result supports the essentiality of a negative charge in IM localization and indicates that the committed step
in lipoprotein sorting is made in a cellular compartment, the periplasm, at equilibrium with the external pH.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Base Sequence</subject><subject>beta-Lactamases - genetics</subject><subject>beta-Lactamases - metabolism</subject><subject>Biological and medical sciences</subject><subject>DNA, Bacterial</subject><subject>Electrochemistry</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - growth & development</subject><subject>Escherichia coli - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Lipoproteins - genetics</subject><subject>Lipoproteins - metabolism</subject><subject>Lipoproteins, myelin</subject><subject>membrane proteins</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis</subject><subject>mutants</subject><subject>periplasmic space</subject><subject>Proteins</subject><subject>Suppression, Genetic</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkEtvFDEQhC1EFDaBnxDJB4TIYYKfs_YRRSEgReJAkLhZtreHaZgZD_as8vj1eNkl8aUPVV3u-gg54-yCM95-KIwJ3lihzXtuzrWWQjT2BVlxZmQjNf_xkqyeLK_ISSm_WH3K8mNyzI3Rem1X5PG2BzrntABOtMCfLUwRaIYyp6lgGIB2KdMB5_TfNMIYsp-ADin6AR_9gmmiVbgqsYeMsUdPYxqQwn2PAZdS40aff_tdWpkhYocRl4fX5KjzQ4E3h3lKvn-6ur383Nx8vf5y-fGmiZq1SyM6AcorZiOE4NsQ1533ayME80JH07aK6xB4gM2GVwrMG6mUscJ42VoIWp6Sd_vc2qD2K4sbsUQYhloibYvjLVNMWlWNem-MOZWSoXNzxnr5g-PM7Zi7bzugbgfUceP-MXe27p0dPtiGETbPW3vIVX970H2pyLpKL2J5silruRby2dbjz_4OM7iAqSIdnWhbJ3Q9VGkj_wJc55it</recordid><startdate>19910905</startdate><enddate>19910905</enddate><creator>GENNITY, J. M</creator><creator>INOUYE, M</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope></search><sort><creationdate>19910905</creationdate><title>The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity</title><author>GENNITY, J. M ; INOUYE, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-2f2e4a409cebba6bc7faa78220a25c866415bb1bedd15530a83448928a369eb53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Base Sequence</topic><topic>beta-Lactamases - genetics</topic><topic>beta-Lactamases - metabolism</topic><topic>Biological and medical sciences</topic><topic>DNA, Bacterial</topic><topic>Electrochemistry</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - growth & development</topic><topic>Escherichia coli - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Lipoproteins - genetics</topic><topic>Lipoproteins - metabolism</topic><topic>Lipoproteins, myelin</topic><topic>membrane proteins</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis</topic><topic>mutants</topic><topic>periplasmic space</topic><topic>Proteins</topic><topic>Suppression, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GENNITY, J. M</creatorcontrib><creatorcontrib>INOUYE, M</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>GENNITY, J. M</au><au>INOUYE, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1991-09-05</date><risdate>1991</risdate><volume>266</volume><issue>25</issue><spage>16458</spage><epage>16464</epage><pages>16458-16464</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Structural information defining an N-terminal sequence required for the membrane sorting of bacterial lipoproteins has been
previously garnered through the study of a hybrid outer membrane (OM) lipo-beta-lactamase (LL) (Ghrayeb and Inouye (1984)
J. Biol. Chem. 259, 463-467). Introduction of an aspartate as the second residue of mature LL (D2 mutant) causes an inner
membrane (IM) localization of this protein (Yamaguchi, K., Yu, F., and Inouye, M. (1988) Cell 53, 423-432). Introduction of
as aspartate at the third residue of mature LL (D3) causes a weaker IM sorting signal and when present as the fourth residue
(D4), normal OM sorting occurs. A positively charged residue at the second position (K2) has no effect on OM localization.
Remarkably, glutamate substitution at either the second (E2) or third (E3) position does not interfere with OM sorting. Sorting
of the mutant D2 LL can be partially suppressed by introduction of a positively charged histidine (D2H3) or lysine (D2K3)
at residue 3 of the mature protein. These results indicate that both the negative charge of the aspartate residue and some
structural feature not present in a glutamate residue are required for sorting to the IM. The suppression of IM localization
of the D2H3 LL double mutant can be eliminated by growing Escherichia coli at pH 8.4 to reduce the histidine partial positive
charge. This result supports the essentiality of a negative charge in IM localization and indicates that the committed step
in lipoprotein sorting is made in a cellular compartment, the periplasm, at equilibrium with the external pH.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1885579</pmid><doi>10.1016/s0021-9258(18)55322-9</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Bacterial Outer Membrane Proteins - metabolism Base Sequence beta-Lactamases - genetics beta-Lactamases - metabolism Biological and medical sciences DNA, Bacterial Electrochemistry Electrophoresis, Polyacrylamide Gel Escherichia coli - genetics Escherichia coli - growth & development Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Lipoproteins - genetics Lipoproteins - metabolism Lipoproteins, myelin membrane proteins Molecular Sequence Data Mutagenesis mutants periplasmic space Proteins Suppression, Genetic |
| title | The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity |
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