<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>1405-888X</journal-id>
<journal-title><![CDATA[TIP. Revista especializada en ciencias químico-biológicas]]></journal-title>
<abbrev-journal-title><![CDATA[TIP]]></abbrev-journal-title>
<issn>1405-888X</issn>
<publisher>
<publisher-name><![CDATA[Universidad Nacional Autónoma de México, Facultad de Estudios Superiores Zaragoza]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S1405-888X2018000321112</article-id>
<article-id pub-id-type="doi">10.22201/fesz.23958723e.2018.0.152</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Regulación de la traducción mediada por la proteína NSP3 de rotavirus]]></article-title>
<article-title xml:lang="en"><![CDATA[Regulation of translation mediated by rotavirus protein NSP3]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Contreras-Treviño]]></surname>
<given-names><![CDATA[Hugo I.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
<xref ref-type="aff" rid="Aaf"/>
<xref ref-type="aff" rid="A a"/>
<xref ref-type="aff" rid="A3"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Padilla-Noriega]]></surname>
<given-names><![CDATA[Luis]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Nacional Autónoma de México Programa de Maestría y Doctorado en Ciencias Bioquímicas ]]></institution>
<addr-line><![CDATA[ Ciudad de México]]></addr-line>
<country>Mexico</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,Universidad Nacional Autónoma de México Instituto de Investigaciones Biomédicas Departamento de Biología Molecular y Biotecnología]]></institution>
<addr-line><![CDATA[ ]]></addr-line>
<country>Mexico</country>
</aff>
<aff id="Af3">
<institution><![CDATA[,Universidad Nacional Autónoma de México Facultad de Medicina Departamento de Microbiología y Parasitología]]></institution>
<addr-line><![CDATA[ ]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>00</month>
<year>2018</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>00</month>
<year>2018</year>
</pub-date>
<volume>21</volume>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S1405-888X2018000321112&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S1405-888X2018000321112&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S1405-888X2018000321112&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen El estudio de los mecanismos utilizados por diversos virus para controlar la traducción de la célula hospedera y favorecer la expresión de proteínas virales ha sido muy instructivo para conocer mecanismos celulares fundamentales que regulan la traducción. La proteína NSP3 de los rotavirus de la especie A (RVA) es capaz de inhibir la traducción de los RNAm celulares como consecuencia de su unión al factor de iniciación de la traducción eIF4G y de estimular la traducción de los RNAm virales como consecuencia de su unión a la secuencia UGACC de su extremo 3&#8217;. Se ha propuesto que NSP3 inhibe la traducción por interferir con la circularización de los extremos 5&#8217;-3&#8217; de los RNAm celulares mediada por eIF4E-eIF4G-PABP (proteína de unión a poli-A), y simultáneamente se propone que NSP3 estimula la traducción de los RNAm del RVA circularizándolos de manera análoga a la que realiza PABP en los RNAm celulares. Sin embargo, la importancia de la dimerización de NSP3 asistida por la chaperona HSP90 en su función inhibitoria de la traducción celular se desconoce. Recientemente, se exploró la importancia de los intermediarios de la dimerización de NSP3 sobre su función inhibitoria de la traducción, y se encontró que mutaciones puntuales en la región coiled-coil afectan la formación de los dímeros y conservan parcialmente su función inhibitoria de la traducción celular. Además, se detectó que los dímeros de NSP3 se degradan con mayor rapidez que los intermediarios de la dimerización. Estos datos demuestran que la función de NSP3 se adquiere previamente a la aparición de los dímeros, y sugiere que la susceptibilidad al proteasoma de las distintas formas oligoméricas de NSP3 son relevantes en el establecimiento de la función inhibitoria de la traducción celular.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract The study of the mechanisms used by different viruses to control host cell translation and favor the expression of viral proteins has been very instructive to know fundamental cellular mechanisms that regulate translation. Species A rotavirus (RVA) NSP3 protein is capable of inhibiting the translation of cellular mRNAs as a consequence of its binding to the translation initiation factor eIF4G and of stimulating the translation of viral mRNAs as a consequence of its binding to the UGACC sequence at their 3&#8217;-end. It has been proposed that NSP3 inhibits translation by interference with the circularization of the 5&#8217;-3&#8217;-ends of cellular mRNAs mediated by eIF4E-eIF4G-PABP (poly-A binding protein), and simultaneously it has been proposed that NSP3 stimulates translation of RVA mRNAs by circularization, in a way analogous to that performed by PABP on cellular mRNAs. However, the importance of NSP3 dimerization assisted by chaperone HSP90 in its inhibitory function of cell translation is unknown. Recently, the importance of NSP3 dimerization intermediates on its inhibitory function on host cell translation was explored, and it was found that point mutations in the coiled-coil region affect the formation of NSP3 dimers and partially preserve its host cell translation inhibitory function. In addition, it was found that NSP3 dimers degrade more rapidly than dimerization intermediates. These data demonstrate that the function of NSP3 is acquired prior to the appearance of dimers and suggests that the proteasome susceptibility of the different oligomeric forms of NSP3 are relevant in the establishment of the inhibitory function of cell translation.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[NSP3]]></kwd>
<kwd lng="es"><![CDATA[intermediarios de dimerización]]></kwd>
<kwd lng="es"><![CDATA[proteostasis]]></kwd>
<kwd lng="es"><![CDATA[inhibición traduccional]]></kwd>
<kwd lng="en"><![CDATA[NSP3]]></kwd>
<kwd lng="en"><![CDATA[dimerization intermediates]]></kwd>
<kwd lng="en"><![CDATA[proteostasis]]></kwd>
<kwd lng="en"><![CDATA[translation inhibition]]></kwd>
</kwd-group>
</article-meta>
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