Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease
The bacterial histidine permease, an ABC transporter, from Salmonella typhimurium is composed of a membrane-bound complex, HisQMP2, comprising two hydrophobic subunits (HisQ and HisM), two copies of an ATP-hydrolyzing subunit, HisP, and a soluble receptor, HisJ. We describe the purification and char...
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| Veröffentlicht in: | Journal of bioenergetics and biomembranes 2001-04, Vol.33 (2), p.79-92 |
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| creator | Ames, G F Nikaido, K Wang, I X Liu, P Q Liu, C E Hu, C |
| description | The bacterial histidine permease, an ABC transporter, from Salmonella typhimurium is composed of a membrane-bound complex, HisQMP2, comprising two hydrophobic subunits (HisQ and HisM), two copies of an ATP-hydrolyzing subunit, HisP, and a soluble receptor, HisJ. We describe the purification and characterization of HisQMP2 using a 6-histidines extension at the carboxy terminus of HisP [HisQMP2(his6)]. The purification is rapid and effective, giving a seven-fold purification with a yield of 85 and 98% purity. Two procedures are described differing in the detergent used (decanoylsucrose and octylglucoside, respectively) and in the presence of phospholipid. HisQMP2(his6) has ATPase and transport activities upon reconstitution into proteoliposomes (PLS). HisQMP2(his6) has a low level ATPase activity (intrinsic activity), which is stimulated to a different extent by the receptor--liganded and unliganded. Its pH optimum is 7.8-8.0, it requires a cation for activity and it displays cooperativity for ATP. The effect of various ATP analogs was analyzed. Determination of the molecular size of HisQMP2(his6) indicates that it is a monomer. The permeability properties of two kinds of reconstituted PLS preparations are described. |
| doi_str_mv | 10.1023/A:1010797029183 |
| format | Article |
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We describe the purification and characterization of HisQMP2 using a 6-histidines extension at the carboxy terminus of HisP [HisQMP2(his6)]. The purification is rapid and effective, giving a seven-fold purification with a yield of 85 and 98% purity. Two procedures are described differing in the detergent used (decanoylsucrose and octylglucoside, respectively) and in the presence of phospholipid. HisQMP2(his6) has ATPase and transport activities upon reconstitution into proteoliposomes (PLS). HisQMP2(his6) has a low level ATPase activity (intrinsic activity), which is stimulated to a different extent by the receptor--liganded and unliganded. Its pH optimum is 7.8-8.0, it requires a cation for activity and it displays cooperativity for ATP. The effect of various ATP analogs was analyzed. Determination of the molecular size of HisQMP2(his6) indicates that it is a monomer. The permeability properties of two kinds of reconstituted PLS preparations are described.</description><identifier>ISSN: 0145-479X</identifier><identifier>EISSN: 1573-6881</identifier><identifier>DOI: 10.1023/A:1010797029183</identifier><identifier>PMID: 11456221</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>ABC transporters ; Adenosine Triphosphatases - chemistry ; Adenosine Triphosphatases - isolation & purification ; Adenosine Triphosphatases - metabolism ; Amino Acid Transport Systems, Basic - chemistry ; Amino Acid Transport Systems, Basic - isolation & purification ; Amino Acid Transport Systems, Basic - metabolism ; ATP ; ATP-Binding Cassette Transporters - chemistry ; ATP-Binding Cassette Transporters - isolation & purification ; ATP-Binding Cassette Transporters - metabolism ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Biological Transport, Active ; Detergents ; Membranes - chemistry ; Molecular Weight ; Permeability ; Phospholipids - pharmacology ; Protein Subunits ; Proteins ; Proteolipids ; Salmonella typhimurium - metabolism ; Solubility</subject><ispartof>Journal of bioenergetics and biomembranes, 2001-04, Vol.33 (2), p.79-92</ispartof><rights>Plenum Publishing Corporation 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c280t-99b1dc2c26fab34d91aa34f65e76ac694e78a3e4dccb39146255f87d66b4b73c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11456221$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ames, G F</creatorcontrib><creatorcontrib>Nikaido, K</creatorcontrib><creatorcontrib>Wang, I X</creatorcontrib><creatorcontrib>Liu, P Q</creatorcontrib><creatorcontrib>Liu, C E</creatorcontrib><creatorcontrib>Hu, C</creatorcontrib><title>Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease</title><title>Journal of bioenergetics and biomembranes</title><addtitle>J Bioenerg Biomembr</addtitle><description>The bacterial histidine permease, an ABC transporter, from Salmonella typhimurium is composed of a membrane-bound complex, HisQMP2, comprising two hydrophobic subunits (HisQ and HisM), two copies of an ATP-hydrolyzing subunit, HisP, and a soluble receptor, HisJ. We describe the purification and characterization of HisQMP2 using a 6-histidines extension at the carboxy terminus of HisP [HisQMP2(his6)]. The purification is rapid and effective, giving a seven-fold purification with a yield of 85 and 98% purity. Two procedures are described differing in the detergent used (decanoylsucrose and octylglucoside, respectively) and in the presence of phospholipid. HisQMP2(his6) has ATPase and transport activities upon reconstitution into proteoliposomes (PLS). HisQMP2(his6) has a low level ATPase activity (intrinsic activity), which is stimulated to a different extent by the receptor--liganded and unliganded. Its pH optimum is 7.8-8.0, it requires a cation for activity and it displays cooperativity for ATP. The effect of various ATP analogs was analyzed. Determination of the molecular size of HisQMP2(his6) indicates that it is a monomer. The permeability properties of two kinds of reconstituted PLS preparations are described.</description><subject>ABC transporters</subject><subject>Adenosine Triphosphatases - chemistry</subject><subject>Adenosine Triphosphatases - isolation & purification</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Amino Acid Transport Systems, Basic - chemistry</subject><subject>Amino Acid Transport Systems, Basic - isolation & purification</subject><subject>Amino Acid Transport Systems, Basic - metabolism</subject><subject>ATP</subject><subject>ATP-Binding Cassette Transporters - chemistry</subject><subject>ATP-Binding Cassette Transporters - isolation & purification</subject><subject>ATP-Binding Cassette Transporters - metabolism</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological Transport, Active</subject><subject>Detergents</subject><subject>Membranes - chemistry</subject><subject>Molecular Weight</subject><subject>Permeability</subject><subject>Phospholipids - pharmacology</subject><subject>Protein Subunits</subject><subject>Proteins</subject><subject>Proteolipids</subject><subject>Salmonella typhimurium - metabolism</subject><subject>Solubility</subject><issn>0145-479X</issn><issn>1573-6881</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkM1LxDAUxIMo7rp69ibFgyer-WiTxtu6-AULelDwVpL0lc3StDVpQf3rzbrrxdODmd88hkHolOArgim7nt8QTLCQAlNJCraHpiQXLOVFQfbRFJMsTzMh3yfoKIQ1xrjAOT5EExINTimZIvcyeltbowbbtYlqq8SslFdmAG-_t2JXJ8MKEgdOe9VCqrtxg3Wub-Bz46o2md8ukiG6oe98jF7-JlY2DLayLSQ9eAcqwDE6qFUT4GR3Z-jt_u518Zgunx-eFvNlamiBh1RKTSpDDeW10iyrJFGKZTXPQXBluMxAFIpBVhmjmSQZp3leF6LiXGdaMMNm6GL7t_fdxwhhKJ0NBpom9u_GUIrNaoXkETz_B6670bexWynySMmc0Aid7aBRO6jK3lun_Ff5tyL7AZEOdNM</recordid><startdate>20010401</startdate><enddate>20010401</enddate><creator>Ames, G F</creator><creator>Nikaido, K</creator><creator>Wang, I X</creator><creator>Liu, P Q</creator><creator>Liu, C E</creator><creator>Hu, C</creator><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20010401</creationdate><title>Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease</title><author>Ames, G F ; Nikaido, K ; Wang, I X ; Liu, P Q ; Liu, C E ; Hu, C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c280t-99b1dc2c26fab34d91aa34f65e76ac694e78a3e4dccb39146255f87d66b4b73c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>ABC transporters</topic><topic>Adenosine Triphosphatases - chemistry</topic><topic>Adenosine Triphosphatases - isolation & purification</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Amino Acid Transport Systems, Basic - chemistry</topic><topic>Amino Acid Transport Systems, Basic - isolation & purification</topic><topic>Amino Acid Transport Systems, Basic - metabolism</topic><topic>ATP</topic><topic>ATP-Binding Cassette Transporters - chemistry</topic><topic>ATP-Binding Cassette Transporters - isolation & purification</topic><topic>ATP-Binding Cassette Transporters - metabolism</topic><topic>Bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biological Transport, Active</topic><topic>Detergents</topic><topic>Membranes - chemistry</topic><topic>Molecular Weight</topic><topic>Permeability</topic><topic>Phospholipids - pharmacology</topic><topic>Protein Subunits</topic><topic>Proteins</topic><topic>Proteolipids</topic><topic>Salmonella typhimurium - metabolism</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ames, G F</creatorcontrib><creatorcontrib>Nikaido, K</creatorcontrib><creatorcontrib>Wang, I X</creatorcontrib><creatorcontrib>Liu, P Q</creatorcontrib><creatorcontrib>Liu, C E</creatorcontrib><creatorcontrib>Hu, C</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of bioenergetics and biomembranes</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ames, G F</au><au>Nikaido, K</au><au>Wang, I X</au><au>Liu, P Q</au><au>Liu, C E</au><au>Hu, C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease</atitle><jtitle>Journal of bioenergetics and biomembranes</jtitle><addtitle>J Bioenerg Biomembr</addtitle><date>2001-04-01</date><risdate>2001</risdate><volume>33</volume><issue>2</issue><spage>79</spage><epage>92</epage><pages>79-92</pages><issn>0145-479X</issn><eissn>1573-6881</eissn><abstract>The bacterial histidine permease, an ABC transporter, from Salmonella typhimurium is composed of a membrane-bound complex, HisQMP2, comprising two hydrophobic subunits (HisQ and HisM), two copies of an ATP-hydrolyzing subunit, HisP, and a soluble receptor, HisJ. We describe the purification and characterization of HisQMP2 using a 6-histidines extension at the carboxy terminus of HisP [HisQMP2(his6)]. The purification is rapid and effective, giving a seven-fold purification with a yield of 85 and 98% purity. Two procedures are described differing in the detergent used (decanoylsucrose and octylglucoside, respectively) and in the presence of phospholipid. HisQMP2(his6) has ATPase and transport activities upon reconstitution into proteoliposomes (PLS). HisQMP2(his6) has a low level ATPase activity (intrinsic activity), which is stimulated to a different extent by the receptor--liganded and unliganded. Its pH optimum is 7.8-8.0, it requires a cation for activity and it displays cooperativity for ATP. The effect of various ATP analogs was analyzed. Determination of the molecular size of HisQMP2(his6) indicates that it is a monomer. The permeability properties of two kinds of reconstituted PLS preparations are described.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>11456221</pmid><doi>10.1023/A:1010797029183</doi><tpages>14</tpages></addata></record> |
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| subjects | ABC transporters Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - isolation & purification Adenosine Triphosphatases - metabolism Amino Acid Transport Systems, Basic - chemistry Amino Acid Transport Systems, Basic - isolation & purification Amino Acid Transport Systems, Basic - metabolism ATP ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - isolation & purification ATP-Binding Cassette Transporters - metabolism Bacteria Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Biological Transport, Active Detergents Membranes - chemistry Molecular Weight Permeability Phospholipids - pharmacology Protein Subunits Proteins Proteolipids Salmonella typhimurium - metabolism Solubility |
| title | Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease |
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