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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The <sc>d</sc>-Xylose-Binding Protein, XylF, from <italic>Thermoanaerobacter ethanolicus</italic> 39E: Cloning, Molecular Analysis, and Expression of the Structural Gene<xref ref-type="fn" rid="FN151">†</xref></title><author><name sortKey="Erbeznik, Milutin" sort="Erbeznik, Milutin" uniqKey="Erbeznik M" first="Milutin" last="Erbeznik">Milutin Erbeznik</name></author><author><name sortKey="Strobel, Herbert J" sort="Strobel, Herbert J" uniqKey="Strobel H" first="Herbert J." last="Strobel">Herbert J. Strobel</name></author><author><name sortKey="Dawson, Karl A" sort="Dawson, Karl A" uniqKey="Dawson K" first="Karl A." last="Dawson">Karl A. Dawson</name></author><author><name sortKey="Jones, Chris R" sort="Jones, Chris R" uniqKey="Jones C" first="Chris R." last="Jones">Chris R. Jones</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">9657999</idno><idno type="pmc">107324</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC107324</idno><idno type="RBID">PMC:107324</idno><date when="1998">1998</date><idno type="wicri:Area/Pmc/Corpus">000021</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000021</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The <sc>d</sc>-Xylose-Binding Protein, XylF, from <italic>Thermoanaerobacter ethanolicus</italic> 39E: Cloning, Molecular Analysis, and Expression of the Structural Gene<xref ref-type="fn" rid="FN151">†</xref></title><author><name sortKey="Erbeznik, Milutin" sort="Erbeznik, Milutin" uniqKey="Erbeznik M" first="Milutin" last="Erbeznik">Milutin Erbeznik</name></author><author><name sortKey="Strobel, Herbert J" sort="Strobel, Herbert J" uniqKey="Strobel H" first="Herbert J." last="Strobel">Herbert J. Strobel</name></author><author><name sortKey="Dawson, Karl A" sort="Dawson, Karl A" uniqKey="Dawson K" first="Karl A." last="Dawson">Karl A. Dawson</name></author><author><name sortKey="Jones, Chris R" sort="Jones, Chris R" uniqKey="Jones C" first="Chris R." last="Jones">Chris R. Jones</name></author></analytic><series><title level="j">Journal of Bacteriology</title><idno type="ISSN">0021-9193</idno><idno type="eISSN">1098-5530</idno><imprint><date when="1998">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Immediately downstream from the <italic>Thermoanaerobacter ethanolicus xylAB</italic> operon, comprising genes that encode <sc>d</sc>-xylose isomerase and <sc>d</sc>-xylulose kinase, lies a 1,101-bp open reading frame that exhibits 61% amino acid sequence identity to the <italic>Escherichia coli</italic> <sc>d</sc>-xylose binding periplasmic receptor, XylF, a component of the high-affinity binding-protein-dependent <sc>d</sc>-xylose transport. The 25-residue N-terminal fragment of the deduced <italic>T. ethanolicus</italic> XylF has typical features of bacterial leader peptides. The C-terminal portion of this leader sequence matches the cleavage consensus for lipoproteins and is followed by a 22-residue putative linker sequence rich in serine, threonine, and asparagine. The putative mature 341-amino-acid-residue XylF (calculated molecular mass of 37,069 Da) appears to be a lipoprotein attached to the cell membrane via a lipid anchor covalently linked to the N-terminal cysteine, as demonstrated by metabolic labelling of the recombinant XylF with [<sup>14</sup>C]palmitate. The induced <italic>E. coli</italic> avidly bound <sc>d</sc>-[<sup>14</sup>C]xylose, yielding additional evidence that <italic>T. ethanolicus</italic> XylF is the <sc>d</sc>-xylose-binding protein. On the basis of sequence comparison of XylFs to other monosaccharide-binding proteins, we propose that the sequence signature of binding proteins specific for hexoses and pentoses be refined as (KDQ)(LIVFAG)<sub>3</sub>IX<sub>3</sub>(DN)(SGP)X<sub>3</sub>(GS)X(LIVA)<sub>2</sub>X<sub>2</sub>A. Transcription of the monocistronic 1.3-kb <italic>xylF</italic> mRNA is inducible by xylose and unaffected by glucose. Primer extension analysis indicated that <italic>xylF</italic> transcription initiates from two +1 sites, both situated within the <italic>xylAB</italic> operon. Unlike in similar transport systems in other bacteria, the genes specifying the membrane components (e.g., ATP-binding protein and permease) of the high-affinity <sc>d</sc>-xylose uptake system are not located in the vicinity of <italic>xylF</italic> in <italic>T. ethanolicus</italic>. This is the first report of a gene encoding a xylose-binding protein in a gram-positive or thermophilic bacterium.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Bacteriol</journal-id><journal-id journal-id-type="publisher-id">J BACTERIOL</journal-id><journal-title>Journal of Bacteriology</journal-title><issn pub-type="ppub">0021-9193</issn><issn pub-type="epub">1098-5530</issn><publisher><publisher-name>American Society for Microbiology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">9657999</article-id><article-id pub-id-type="pmc">107324</article-id><article-id pub-id-type="publisher-id">0129</article-id><article-categories><subj-group subj-group-type="heading"><subject>Enzymes and Proteins</subject></subj-group></article-categories><title-group><article-title>The <sc>d</sc>-Xylose-Binding Protein, XylF, from <italic>Thermoanaerobacter ethanolicus</italic> 39E: Cloning, Molecular Analysis, and Expression of the Structural Gene<xref ref-type="fn" rid="FN151">†</xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Erbeznik</surname><given-names>Milutin</given-names></name><xref ref-type="author-notes" rid="FN152">‡</xref></contrib><contrib contrib-type="author"><name><surname>Strobel</surname><given-names>Herbert J.</given-names></name><xref ref-type="author-notes" rid="FN150">*</xref></contrib><contrib contrib-type="author"><name><surname>Dawson</surname><given-names>Karl A.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Jones</surname><given-names>Chris R.</given-names></name></contrib></contrib-group><aff id="N0x9750900.0x9cd0320">Department of Animal Sciences, University of Kentucky, Lexington, Kentucky 40546-0215</aff><author-notes><fn id="FN150"><label>*</label><p>Corresponding author. Mailing address: 212 W. P. Garrigus Building, Department of Animal Sciences, University of Kentucky, Lexington, KY 40546-0215. Phone: (606) 257-7554. Fax: (606) 257-5318. E-mail: <email>strobel@pop.uky.edu</email>.</p></fn><fn id="FN152"><label>‡</label><p>Present address: Department of Biochemistry, Chandler Medical Center, University of Kentucky, Lexington, KY 40536-0084.</p></fn></author-notes><pub-date pub-type="ppub"><month>7</month><year>1998</year></pub-date><volume>180</volume><issue>14</issue><fpage>3570</fpage><lpage>3577</lpage><history><date date-type="received"><day>3</day><month>2</month><year>1998</year></date><date date-type="accepted"><day>15</day><month>5</month><year>1998</year></date></history><copyright-statement>Copyright © 1998, American Society for Microbiology</copyright-statement><copyright-year>1998</copyright-year><abstract><p>Immediately downstream from the <italic>Thermoanaerobacter ethanolicus xylAB</italic> operon, comprising genes that encode <sc>d</sc>-xylose isomerase and <sc>d</sc>-xylulose kinase, lies a 1,101-bp open reading frame that exhibits 61% amino acid sequence identity to the <italic>Escherichia coli</italic> <sc>d</sc>-xylose binding periplasmic receptor, XylF, a component of the high-affinity binding-protein-dependent <sc>d</sc>-xylose transport. The 25-residue N-terminal fragment of the deduced <italic>T. ethanolicus</italic> XylF has typical features of bacterial leader peptides. The C-terminal portion of this leader sequence matches the cleavage consensus for lipoproteins and is followed by a 22-residue putative linker sequence rich in serine, threonine, and asparagine. The putative mature 341-amino-acid-residue XylF (calculated molecular mass of 37,069 Da) appears to be a lipoprotein attached to the cell membrane via a lipid anchor covalently linked to the N-terminal cysteine, as demonstrated by metabolic labelling of the recombinant XylF with [<sup>14</sup>C]palmitate. The induced <italic>E. coli</italic> avidly bound <sc>d</sc>-[<sup>14</sup>C]xylose, yielding additional evidence that <italic>T. ethanolicus</italic> XylF is the <sc>d</sc>-xylose-binding protein. On the basis of sequence comparison of XylFs to other monosaccharide-binding proteins, we propose that the sequence signature of binding proteins specific for hexoses and pentoses be refined as (KDQ)(LIVFAG)<sub>3</sub>IX<sub>3</sub>(DN)(SGP)X<sub>3</sub>(GS)X(LIVA)<sub>2</sub>X<sub>2</sub>A. Transcription of the monocistronic 1.3-kb <italic>xylF</italic> mRNA is inducible by xylose and unaffected by glucose. Primer extension analysis indicated that <italic>xylF</italic> transcription initiates from two +1 sites, both situated within the <italic>xylAB</italic> operon. Unlike in similar transport systems in other bacteria, the genes specifying the membrane components (e.g., ATP-binding protein and permease) of the high-affinity <sc>d</sc>-xylose uptake system are not located in the vicinity of <italic>xylF</italic> in <italic>T. ethanolicus</italic>. This is the first report of a gene encoding a xylose-binding protein in a gram-positive or thermophilic bacterium.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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