<?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>2594-1925</journal-id>
<journal-title><![CDATA[Revista de ciencias tecnológicas]]></journal-title>
<abbrev-journal-title><![CDATA[Rev. cienc. tecnol.]]></abbrev-journal-title>
<issn>2594-1925</issn>
<publisher>
<publisher-name><![CDATA[Universidad Autónoma de Baja California]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S2594-19252024000400105</article-id>
<article-id pub-id-type="doi">10.37636/recit.v7n4e372</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Predicción estructural y funcional de las ADN glicosilasas así como su relación filogenética por métodos bioinformáticos]]></article-title>
<article-title xml:lang="en"><![CDATA[Structural and functional prediction of DNA glycosylases as well as their phylogenetic relationship by bioinformatic methods]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Pinkney-Rivas]]></surname>
<given-names><![CDATA[Estrella Alejandra]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Popoca-Cuaya]]></surname>
<given-names><![CDATA[Marco Antonio]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Autónoma de Campeche Facultad de Ciencias Químico Biológicas ]]></institution>
<addr-line><![CDATA[Campeche Campeche]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>12</month>
<year>2024</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>12</month>
<year>2024</year>
</pub-date>
<volume>7</volume>
<numero>4</numero>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S2594-19252024000400105&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S2594-19252024000400105&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S2594-19252024000400105&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen. Las bases nitrogenadas que conforman a los nucleótidos del ADN pueden ser alteradas por factores externos e internos. El mecanismo de reparación por escisión de bases (BER) se encarga de remover las bases dañadas a través de un conjunto de enzimas. En este trabajo realizamos un análisis in silico de las secuencias de los genes y proteínas de las glicosilasas encargadas de eliminar las bases alteradas: MPG, OGG1, NEIL1, MUTYH y NTHL1 que participan en la reparación por el mecanismo de BER de Homo sapiens. Utilizamos diferentes softwares bioinformáticos con el objetivo de caracterizar el contenido de guanina y citocina (G&#8801;C) de los genes, las estructuras secundarias y terciaria de las glicosilasas, los motivos en las proteínas, así como la relación filogenética entre las glicosilasas. Las secuencias de los genes y de los aminoácidos se descargaron del GeneBank, se utilizaron los softwares en línea GENSCAN, Gor4, phyre2, InterPro y MEGA. El contenido G&#8801;C obtenido en porcentaje fueron de 63.80%, 63.50%, 61.33%, 60.48% y 59.20% para MPG, NTHL1, NEIL1, MUTYH y OGG1 respectivamente. La estructura secundaria de las proteínas mostró que NTHL1 tiene el porcentaje más alto (43.42%) de alfa hélice, OGG1(16.23%) en la estructura de cadena extendida y NEIL1 en el plegamiento aleatorio (57.69%). Adicionalmente se realizó la predicción de la estructura terciaria y de los dominios en las proteínas, el dominio HhH está presente en OGG1, MUTYH y NTHL1. El árbol filogenético mostró la relación evolutiva entre los genes estudiados, siendo el gen OGG1 el ancestro común. Los resultados de las predicciones son importantes para comprender la estructura molecular de las glicosilasas, además la información generada puede ser utilizados tanto en estudios experimentales, biotecnológicos y en la función evolutiva durante la reparación del ADN y en el diseño de estrategias terapéuticas en las cuales están involucradas las glicosilasas.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract. Nitrogenous bases are a component of DNA nucleotides and can be altered by both external and internal factors. The base excision repair (BER) mechanism is responsible for removing damaged bases through the action of various enzymes. In this study, we performed an in-silico analysis of the gene and protein sequences of glycosylases responsible for eliminating altered bases: MPG, OGG1, NEIL1, MUTYH, and NTHL1, which participate in the BER mechanism of Homo sapiens. We used various bioinformatics tools to characterize the guanine and cytosine (G&#8801;C) content of the genes, the secondary and tertiary structures of the glycosylases, protein motifs, and the phylogenetic relationships between the glycosylases. Gene and amino acid sequences were downloaded from GenBank, and the online software tools GENSCAN, Gor4, Phyre2, InterPro, and MEGA were used. The G&#8801;C content percentages obtained were 63.80%, 63.50%, 61.33%, 60.48%, and 59.20% for MPG, NTHL1, NEIL1, MUTYH, and OGG1, respectively. Secondary structure analysis of the proteins showed that NTHL1 has the highest percentage (43.42%) of alpha helix, OGG1 has the highest percentage (16.23%) of extended chain structure, and NEIL1 has the highest percentage of random coil (57.69%). Additionally, we performed the prediction of tertiary structure and domains in proteins, where the HhH domain was observed in OGG1, MUTYH, and NTHL1. The phylogenetic tree revealed the evolutionary relationships among the studied genes, with the OGG1 gene being the common ancestor. These findings are important for understanding the molecular structure of glycosylases and provide valuable information that can be utilized in both experimental and biotechnological studies, as well as in understanding the evolutionary function of DNA repair and in the design of therapeutic strategies involving glycosylases.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[Estrés oxidativo]]></kwd>
<kwd lng="es"><![CDATA[Genotoxicidad]]></kwd>
<kwd lng="es"><![CDATA[Reparación]]></kwd>
<kwd lng="es"><![CDATA[ADN]]></kwd>
<kwd lng="es"><![CDATA[in silico]]></kwd>
<kwd lng="en"><![CDATA[Oxidative stress]]></kwd>
<kwd lng="en"><![CDATA[Genotoxicity]]></kwd>
<kwd lng="en"><![CDATA[Repair]]></kwd>
<kwd lng="en"><![CDATA[DNA]]></kwd>
<kwd lng="en"><![CDATA[in silico]]></kwd>
</kwd-group>
</article-meta>
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