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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>
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