<?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>S1405-888X2023000100216</article-id>
<article-id pub-id-type="doi">10.22201/fesz.23958723e.2023.617</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[El AB&#8220;Y&#8221; de la fosforilación de tirosinas en bacterias: descripción de las enzimas implicadas y su impacto en la fisiología procarionte]]></article-title>
<article-title xml:lang="en"><![CDATA[AB&#8220;Y&#8221; of bacterial tyrosine phosphorylation: description of contributing enzymes and its impact in bacterial physiology]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Andrade]]></surname>
<given-names><![CDATA[Ángel]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Alonso]]></surname>
<given-names><![CDATA[Óscar M.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Tavares-Carreón]]></surname>
<given-names><![CDATA[Faviola]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Autónoma de Nuevo León Facultad de Medicina Departamento de Microbiología]]></institution>
<addr-line><![CDATA[Monterrey Nuevo León]]></addr-line>
<country>México</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,Universidad Autónoma de Nuevo León Facultad de Ciencias Biológicas ]]></institution>
<addr-line><![CDATA[San Nicolás de los Garza Nuevo León]]></addr-line>
<country>México</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>00</month>
<year>2023</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>00</month>
<year>2023</year>
</pub-date>
<volume>26</volume>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S1405-888X2023000100216&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S1405-888X2023000100216&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S1405-888X2023000100216&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen La fosforilación de proteínas en residuos de serina, treonina y tirosina representa un paradigma central de la señalización celular. No obstante, en procariontes esta modificación postraduccional (MPT) fue desestimada durante varias décadas. Diversos estudios fosfoproteómicos bacterianos, así como la identificación y caracterización exhaustiva de las enzimas responsables de la fosforilación de proteínas en estos organismos ha derivado en una nueva visión del alcance regulatorio asociado a esta MPT. En particular, esta revisión se centra en la fosforilación en residuos de tirosina, las enzimas cinasas y fosfatasas implicadas en este proceso, su mecanismo de acción y el impacto de su actividad sobre la fisiología bacteriana.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract Protein phosphorylation in serine, threonine and tyrosine residues is a central paradigm in cell signaling. However, in prokaryotes this post-translational modification (PTM) was dismissed until last two decades. Several bacterial phosphoproteomic studies along with identification and characterization of the enzymes responsible of protein phosphorylation in these organisms, has triggered a fresh view on the research area pointing out to this PTM as an important regulatory mechanism in bacteria. Particularly, in this review we will focus on tyrosine phosphorylation, the kinases and phosphatases achieving incorporation and removal of phosphate moiety, and their mechanism of action and impact on the bacterial physiology.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[fosforilación en tirosinas]]></kwd>
<kwd lng="es"><![CDATA[tirosina cinasa bacteriana]]></kwd>
<kwd lng="es"><![CDATA[tirosina fosfatasa]]></kwd>
<kwd lng="en"><![CDATA[tyrosine phosphorylation]]></kwd>
<kwd lng="en"><![CDATA[bacterial tyrosine kinase]]></kwd>
<kwd lng="en"><![CDATA[tyrosine phosphatase]]></kwd>
</kwd-group>
</article-meta>
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