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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Evolution of arylalkylamine <italic>N</italic>-acetyltransferase: Emergence and divergence</title><author><name sortKey="Coon, Steven L" sort="Coon, Steven L" uniqKey="Coon S" first="Steven L." last="Coon">Steven L. Coon</name></author><author><name sortKey="Klein, David C" sort="Klein, David C" uniqKey="Klein D" first="David C." last="Klein">David C. Klein</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16697105</idno><idno type="pmc">1578506</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1578506</idno><idno type="RBID">PMC:1578506</idno><idno type="doi">10.1016/S0303-7207(06)00135-3</idno><date when="2006">2006</date><idno type="wicri:Area/Pmc/Corpus">000035</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000035</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Evolution of arylalkylamine <italic>N</italic>-acetyltransferase: Emergence and divergence</title><author><name sortKey="Coon, Steven L" sort="Coon, Steven L" uniqKey="Coon S" first="Steven L." last="Coon">Steven L. Coon</name></author><author><name sortKey="Klein, David C" sort="Klein, David C" uniqKey="Klein D" first="David C." last="Klein">David C. Klein</name></author></analytic><series><title level="j">Molecular and cellular endocrinology</title><idno type="ISSN">0303-7207</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">The melatonin rhythm-generating enzyme, arylalkylamine <italic>N</italic>-acetyltransferase (AANAT) is known to have recognizable ancient homologs in bacteria and fungi, but not in other eukaryotes. Analysis of new cDNA and genomic sequences has identified several additional homologs in other groupings. First, an AANAT homolog has been found in the genome of the cephalochordate amphioxus, representing the oldest homolog in chordates. Second, two AANAT homologs have been identified in unicellular green algae. The homologs in amphioxus, unicellular green algae, fungi and bacteria are similarly primitive in that they lack sequences found in vertebrate AANATs that are involved in regulation and that facilitate binding and catalysis. In addition, all these sequences are intronless. These features are consistent with horizontal transfer of the AANAT ancestor from bacteria to green algae, fungi and chordates. Lastly, a third AANAT gene has been found in teleost fish, suggesting that AANAT genes serve multiple functions in addition to melatonin synthesis.</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>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">7500844</journal-id><journal-id journal-id-type="pubmed-jr-id">3382</journal-id><journal-id journal-id-type="nlm-ta">Mol Cell Endocrinol</journal-id><journal-title>Molecular and cellular endocrinology</journal-title><issn pub-type="ppub">0303-7207</issn></journal-meta><article-meta><article-id pub-id-type="pmid">16697105</article-id><article-id pub-id-type="pmc">1578506</article-id><article-id pub-id-type="doi">10.1016/S0303-7207(06)00135-3</article-id><article-id pub-id-type="manuscript">NIHMS11401</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Evolution of arylalkylamine <italic>N</italic>-acetyltransferase: Emergence and divergence</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Coon</surname><given-names>Steven L.</given-names></name><xref rid="FN1" ref-type="author-notes">*</xref></contrib><contrib contrib-type="author"><name><surname>Klein</surname><given-names>David C.</given-names></name></contrib><aff id="A1">Section on Neuroendocrinology, Office of the Scientific Director, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20894, USA</aff></contrib-group><author-notes><corresp id="FN1">*Corresponding author. Tel.: (301) 451-6622; fax: (301) 480-3526, <italic>E-mail address:</italic> <email>coons@mail.nih.gov</email> (S.L. Coon)</corresp></author-notes><pub-date pub-type="nihms-submitted"><day>28</day><month>8</month><year>2006</year></pub-date><pub-date pub-type="epub"><day>11</day><month>5</month><year>2006</year></pub-date><pub-date pub-type="ppub"><day>27</day><month>6</month><year>2006</year></pub-date><pub-date pub-type="pmc-release"><day>27</day><month>6</month><year>2007</year></pub-date><volume>252</volume><issue>1-2</issue><fpage>2</fpage><lpage>10</lpage><abstract><p id="P1">The melatonin rhythm-generating enzyme, arylalkylamine <italic>N</italic>-acetyltransferase (AANAT) is known to have recognizable ancient homologs in bacteria and fungi, but not in other eukaryotes. Analysis of new cDNA and genomic sequences has identified several additional homologs in other groupings. First, an AANAT homolog has been found in the genome of the cephalochordate amphioxus, representing the oldest homolog in chordates. Second, two AANAT homologs have been identified in unicellular green algae. The homologs in amphioxus, unicellular green algae, fungi and bacteria are similarly primitive in that they lack sequences found in vertebrate AANATs that are involved in regulation and that facilitate binding and catalysis. In addition, all these sequences are intronless. These features are consistent with horizontal transfer of the AANAT ancestor from bacteria to green algae, fungi and chordates. Lastly, a third AANAT gene has been found in teleost fish, suggesting that AANAT genes serve multiple functions in addition to melatonin synthesis.</p></abstract><kwd-group><kwd>arylalkylamine <italic>N</italic>-acetyltransferase</kwd><kwd>AANAT</kwd><kwd>evolution</kwd><kwd>melatonin</kwd></kwd-group><contract-num rid="PHS2">001-0174-441</contract-num><contract-sponsor id="PHS2">NIH Intramural Employee : PHS</contract-sponsor></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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