Evidence for the Transport of Maltose by the Sucrose Permease, CscB, of Escherichia coli
The purpose of this study was to examine the sugar recognition and transport properties of the sucrose permease (CscB), a secondary active transporter from Escherichia coli. We tested the hypothesis that maltose transport is conferred by the wild-type CscB transporter. Cells of E. coli HS4006 harbor...
Gespeichert in:
| Veröffentlicht in: | The Journal of membrane biology 2009-03, Vol.228 (2), p.79-88 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 88 |
|---|---|
| container_issue | 2 |
| container_start_page | 79 |
| container_title | The Journal of membrane biology |
| container_volume | 228 |
| creator | Peng, Yang Kumar, Sanath Hernandez, Ricardo L Jones, Suzanna E Cadle, Kathleen M Smith, Kenneth P Varela, Manuel F |
| description | The purpose of this study was to examine the sugar recognition and transport properties of the sucrose permease (CscB), a secondary active transporter from Escherichia coli. We tested the hypothesis that maltose transport is conferred by the wild-type CscB transporter. Cells of E. coli HS4006 harboring pSP72/cscB were red on maltose MacConkey agar indicator plates. We were able to measure “downhill” maltose transport and establish definitive kinetic behavior for maltose entry in such cells. Maltose was an effective competitor of sucrose transport in cells with CscB, suggesting that the respective maltose and sucrose binding sites and translocation pathways through the CscB channel overlap. Accumulation (“uphill” transport) of maltose by cells with CscB was profound, demonstrating active transport of maltose by CscB. Sequencing of cscB encoded on plasmid pSP72/cscB used in cells for transport studies indicate an unaltered primary CscB structure, ruling out the possibility that mutation conferred maltose transport by CscB. We conclude that maltose is a bona fide substrate for the sucrose permease of E. coli. Thus, future studies of sugar binding, transport, and permease structure should consider maltose, as well as sucrose. |
| doi_str_mv | 10.1007/s00232-009-9161-9 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2661012</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1667653071</sourcerecordid><originalsourceid>FETCH-LOGICAL-c522t-2818eee30d741221d69b73d611e900dbbb060d5f253d591b68b73ecc93a1e7f3</originalsourceid><addsrcrecordid>eNqFkUtv1DAUhSMEotPCD2ADEYuuGvC9fmS8QYLR8JCKQOogsbMc52YmVSae2kml_nscMqLAAlaWfb5zbN-TZc-AvQLGyteRMeRYMKYLDQoK_SBbgEgnIFA8zBZJxgIVh5PsNMZrxqAslXicnYBGLYSERfZ9fdvW1DvKGx_yYUf5Jtg-HnwYct_kn203-Eh5dfdTuxpdmLZfKezJRrrIV9G9u5jIdXQ7Cq3btTZ3vmufZI8a20V6elzPss379Wb1sbj88uHT6u1l4STiUOASlkTEWV0KQIRa6arktQIgzVhdVRVTrJYNSl5LDZVaJpmc09wClQ0_y97MsYex2lPtqB-C7cwhtHsb7oy3rflT6dud2fpbg0oBA0wB58eA4G9GioPZt9FR19me_BiNKpnkGpf_BZHJpQYpEvjyL_Daj6FPQzAIpZASS0gQzNA00Bio-fVkYGYq18zlmlSumco1Onme__7Xe8exzQTgDMQk9VsK9zf_K_XFbGqsN3Yb2mi-XSEDzpIOXCD_Ad-ht4c</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217455271</pqid></control><display><type>article</type><title>Evidence for the Transport of Maltose by the Sucrose Permease, CscB, of Escherichia coli</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>Peng, Yang ; Kumar, Sanath ; Hernandez, Ricardo L ; Jones, Suzanna E ; Cadle, Kathleen M ; Smith, Kenneth P ; Varela, Manuel F</creator><creatorcontrib>Peng, Yang ; Kumar, Sanath ; Hernandez, Ricardo L ; Jones, Suzanna E ; Cadle, Kathleen M ; Smith, Kenneth P ; Varela, Manuel F</creatorcontrib><description>The purpose of this study was to examine the sugar recognition and transport properties of the sucrose permease (CscB), a secondary active transporter from Escherichia coli. We tested the hypothesis that maltose transport is conferred by the wild-type CscB transporter. Cells of E. coli HS4006 harboring pSP72/cscB were red on maltose MacConkey agar indicator plates. We were able to measure “downhill” maltose transport and establish definitive kinetic behavior for maltose entry in such cells. Maltose was an effective competitor of sucrose transport in cells with CscB, suggesting that the respective maltose and sucrose binding sites and translocation pathways through the CscB channel overlap. Accumulation (“uphill” transport) of maltose by cells with CscB was profound, demonstrating active transport of maltose by CscB. Sequencing of cscB encoded on plasmid pSP72/cscB used in cells for transport studies indicate an unaltered primary CscB structure, ruling out the possibility that mutation conferred maltose transport by CscB. We conclude that maltose is a bona fide substrate for the sucrose permease of E. coli. Thus, future studies of sugar binding, transport, and permease structure should consider maltose, as well as sucrose.</description><identifier>ISSN: 0022-2631</identifier><identifier>EISSN: 1432-1424</identifier><identifier>DOI: 10.1007/s00232-009-9161-9</identifier><identifier>PMID: 19294451</identifier><language>eng</language><publisher>New York: New York : Springer-Verlag</publisher><subject>Amino Acid Sequence ; Binding sites ; Biochemistry ; Biological Transport ; Biomedical and Life Sciences ; Cellular biology ; E coli ; Escherichia coli ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Human Physiology ; Kinetics ; Life Sciences ; Maltose - metabolism ; Membrane Transport Proteins - genetics ; Membrane Transport Proteins - metabolism ; Membranes ; Molecular Sequence Data ; Mutation ; Sequence Homology, Amino Acid ; Sucrose - metabolism ; Sugar</subject><ispartof>The Journal of membrane biology, 2009-03, Vol.228 (2), p.79-88</ispartof><rights>Springer Science+Business Media, LLC 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-2818eee30d741221d69b73d611e900dbbb060d5f253d591b68b73ecc93a1e7f3</citedby><cites>FETCH-LOGICAL-c522t-2818eee30d741221d69b73d611e900dbbb060d5f253d591b68b73ecc93a1e7f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00232-009-9161-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00232-009-9161-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19294451$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Peng, Yang</creatorcontrib><creatorcontrib>Kumar, Sanath</creatorcontrib><creatorcontrib>Hernandez, Ricardo L</creatorcontrib><creatorcontrib>Jones, Suzanna E</creatorcontrib><creatorcontrib>Cadle, Kathleen M</creatorcontrib><creatorcontrib>Smith, Kenneth P</creatorcontrib><creatorcontrib>Varela, Manuel F</creatorcontrib><title>Evidence for the Transport of Maltose by the Sucrose Permease, CscB, of Escherichia coli</title><title>The Journal of membrane biology</title><addtitle>J Membrane Biol</addtitle><addtitle>J Membr Biol</addtitle><description>The purpose of this study was to examine the sugar recognition and transport properties of the sucrose permease (CscB), a secondary active transporter from Escherichia coli. We tested the hypothesis that maltose transport is conferred by the wild-type CscB transporter. Cells of E. coli HS4006 harboring pSP72/cscB were red on maltose MacConkey agar indicator plates. We were able to measure “downhill” maltose transport and establish definitive kinetic behavior for maltose entry in such cells. Maltose was an effective competitor of sucrose transport in cells with CscB, suggesting that the respective maltose and sucrose binding sites and translocation pathways through the CscB channel overlap. Accumulation (“uphill” transport) of maltose by cells with CscB was profound, demonstrating active transport of maltose by CscB. Sequencing of cscB encoded on plasmid pSP72/cscB used in cells for transport studies indicate an unaltered primary CscB structure, ruling out the possibility that mutation conferred maltose transport by CscB. We conclude that maltose is a bona fide substrate for the sucrose permease of E. coli. Thus, future studies of sugar binding, transport, and permease structure should consider maltose, as well as sucrose.</description><subject>Amino Acid Sequence</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biological Transport</subject><subject>Biomedical and Life Sciences</subject><subject>Cellular biology</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Human Physiology</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Maltose - metabolism</subject><subject>Membrane Transport Proteins - genetics</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>Membranes</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sucrose - metabolism</subject><subject>Sugar</subject><issn>0022-2631</issn><issn>1432-1424</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkUtv1DAUhSMEotPCD2ADEYuuGvC9fmS8QYLR8JCKQOogsbMc52YmVSae2kml_nscMqLAAlaWfb5zbN-TZc-AvQLGyteRMeRYMKYLDQoK_SBbgEgnIFA8zBZJxgIVh5PsNMZrxqAslXicnYBGLYSERfZ9fdvW1DvKGx_yYUf5Jtg-HnwYct_kn203-Eh5dfdTuxpdmLZfKezJRrrIV9G9u5jIdXQ7Cq3btTZ3vmufZI8a20V6elzPss379Wb1sbj88uHT6u1l4STiUOASlkTEWV0KQIRa6arktQIgzVhdVRVTrJYNSl5LDZVaJpmc09wClQ0_y97MsYex2lPtqB-C7cwhtHsb7oy3rflT6dud2fpbg0oBA0wB58eA4G9GioPZt9FR19me_BiNKpnkGpf_BZHJpQYpEvjyL_Daj6FPQzAIpZASS0gQzNA00Bio-fVkYGYq18zlmlSumco1Onme__7Xe8exzQTgDMQk9VsK9zf_K_XFbGqsN3Yb2mi-XSEDzpIOXCD_Ad-ht4c</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>Peng, Yang</creator><creator>Kumar, Sanath</creator><creator>Hernandez, Ricardo L</creator><creator>Jones, Suzanna E</creator><creator>Cadle, Kathleen M</creator><creator>Smith, Kenneth P</creator><creator>Varela, Manuel F</creator><general>New York : Springer-Verlag</general><general>Springer-Verlag</general><general>Springer Nature B.V</general><scope>FBQ</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>3V.</scope><scope>7RV</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</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>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>PDBOC</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090301</creationdate><title>Evidence for the Transport of Maltose by the Sucrose Permease, CscB, of Escherichia coli</title><author>Peng, Yang ; Kumar, Sanath ; Hernandez, Ricardo L ; Jones, Suzanna E ; Cadle, Kathleen M ; Smith, Kenneth P ; Varela, Manuel F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c522t-2818eee30d741221d69b73d611e900dbbb060d5f253d591b68b73ecc93a1e7f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Binding sites</topic><topic>Biochemistry</topic><topic>Biological Transport</topic><topic>Biomedical and Life Sciences</topic><topic>Cellular biology</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Human Physiology</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Maltose - metabolism</topic><topic>Membrane Transport Proteins - genetics</topic><topic>Membrane Transport Proteins - metabolism</topic><topic>Membranes</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sucrose - metabolism</topic><topic>Sugar</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Peng, Yang</creatorcontrib><creatorcontrib>Kumar, Sanath</creatorcontrib><creatorcontrib>Hernandez, Ricardo L</creatorcontrib><creatorcontrib>Jones, Suzanna E</creatorcontrib><creatorcontrib>Cadle, Kathleen M</creatorcontrib><creatorcontrib>Smith, Kenneth P</creatorcontrib><creatorcontrib>Varela, Manuel F</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Nursing & Allied Health Database</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>ProQuest Pharma Collection</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>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>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Materials Science Collection</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of membrane biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Peng, Yang</au><au>Kumar, Sanath</au><au>Hernandez, Ricardo L</au><au>Jones, Suzanna E</au><au>Cadle, Kathleen M</au><au>Smith, Kenneth P</au><au>Varela, Manuel F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for the Transport of Maltose by the Sucrose Permease, CscB, of Escherichia coli</atitle><jtitle>The Journal of membrane biology</jtitle><stitle>J Membrane Biol</stitle><addtitle>J Membr Biol</addtitle><date>2009-03-01</date><risdate>2009</risdate><volume>228</volume><issue>2</issue><spage>79</spage><epage>88</epage><pages>79-88</pages><issn>0022-2631</issn><eissn>1432-1424</eissn><abstract>The purpose of this study was to examine the sugar recognition and transport properties of the sucrose permease (CscB), a secondary active transporter from Escherichia coli. We tested the hypothesis that maltose transport is conferred by the wild-type CscB transporter. Cells of E. coli HS4006 harboring pSP72/cscB were red on maltose MacConkey agar indicator plates. We were able to measure “downhill” maltose transport and establish definitive kinetic behavior for maltose entry in such cells. Maltose was an effective competitor of sucrose transport in cells with CscB, suggesting that the respective maltose and sucrose binding sites and translocation pathways through the CscB channel overlap. Accumulation (“uphill” transport) of maltose by cells with CscB was profound, demonstrating active transport of maltose by CscB. Sequencing of cscB encoded on plasmid pSP72/cscB used in cells for transport studies indicate an unaltered primary CscB structure, ruling out the possibility that mutation conferred maltose transport by CscB. We conclude that maltose is a bona fide substrate for the sucrose permease of E. coli. Thus, future studies of sugar binding, transport, and permease structure should consider maltose, as well as sucrose.</abstract><cop>New York</cop><pub>New York : Springer-Verlag</pub><pmid>19294451</pmid><doi>10.1007/s00232-009-9161-9</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2631 |
| ispartof | The Journal of membrane biology, 2009-03, Vol.228 (2), p.79-88 |
| issn | 0022-2631 1432-1424 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2661012 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Amino Acid Sequence Binding sites Biochemistry Biological Transport Biomedical and Life Sciences Cellular biology E coli Escherichia coli Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Human Physiology Kinetics Life Sciences Maltose - metabolism Membrane Transport Proteins - genetics Membrane Transport Proteins - metabolism Membranes Molecular Sequence Data Mutation Sequence Homology, Amino Acid Sucrose - metabolism Sugar |
| title | Evidence for the Transport of Maltose by the Sucrose Permease, CscB, of Escherichia coli |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-14T22%3A50%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Evidence%20for%20the%20Transport%20of%20Maltose%20by%20the%20Sucrose%20Permease,%20CscB,%20of%20Escherichia%20coli&rft.jtitle=The%20Journal%20of%20membrane%20biology&rft.au=Peng,%20Yang&rft.date=2009-03-01&rft.volume=228&rft.issue=2&rft.spage=79&rft.epage=88&rft.pages=79-88&rft.issn=0022-2631&rft.eissn=1432-1424&rft_id=info:doi/10.1007/s00232-009-9161-9&rft_dat=%3Cproquest_pubme%3E1667653071%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=217455271&rft_id=info:pmid/19294451&rfr_iscdi=true |