<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-09-15T18:20:39Z</responseDate><request verb="GetRecord" identifier="oai:gredos.usal.es:10366/156861" metadataPrefix="mods">https://gredos.usal.es/oai/request</request><GetRecord><record><header><identifier>oai:gredos.usal.es:10366/156861</identifier><datestamp>2025-04-30T20:42:07Z</datestamp><setSpec>com_10366_156461</setSpec><setSpec>com_10366_4512</setSpec><setSpec>com_10366_3823</setSpec><setSpec>col_10366_156462</setSpec></header><metadata><mods:mods xmlns:mods="http://www.loc.gov/mods/v3" xmlns:doc="http://www.lyncode.com/xoai" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-1.xsd">
<mods:name>
<mods:namePart>Albornos, Lucía</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Martín Sánchez, José Ignacio</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Iglesias, Rebeca</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Jiménez, Teresa</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Labrador, Emilia</mods:namePart>
</mods:name>
<mods:name>
<mods:namePart>Dopico, Berta</mods:namePart>
</mods:name>
<mods:extension>
<mods:dateAvailable encoding="iso8601">2024-03-21T11:22:19Z</mods:dateAvailable>
</mods:extension>
<mods:extension>
<mods:dateAccessioned encoding="iso8601">2024-03-21T11:22:19Z</mods:dateAccessioned>
</mods:extension>
<mods:originInfo>
<mods:dateIssued encoding="iso8601">2012</mods:dateIssued>
</mods:originInfo>
<mods:identifier type="uri">http://hdl.handle.net/10366/156861</mods:identifier>
<mods:identifier type="doi">10.1186/1471-2229-12-207</mods:identifier>
<mods:identifier type="essn">1471-2229</mods:identifier>
<mods:abstract>Background: Many proteins with tandem repeats in their sequence have been described and classified according&#xd;
to the length of the repeats: I) Repeats of short oligopeptides (from 2 to 20 amino acids), including structural cell&#xd;
wall proteins and arabinogalactan proteins. II) Repeats that range in length from 20 to 40 residues, including&#xd;
proteins with a well-established three-dimensional structure often involved in mediating protein-protein&#xd;
interactions. (III) Longer repeats in the order of 100 amino acids that constitute structurally and functionally&#xd;
independent units. Here we analyse ShooT specific (ST) proteins, a family of proteins with tandem repeats of&#xd;
unknown function that were first found in Leguminosae, and their possible similarities to other proteins with&#xd;
tandem repeats.&#xd;
Results: ST protein sequences were only found in dicotyledonous plants, limited to several plant families, mainly&#xd;
the Fabaceae and the Asteraceae. ST mRNAs accumulate mainly in the roots and under biotic interactions. Most ST&#xd;
proteins have one or several Domain(s) of Unknown Function 2775 (DUF2775). All deduced ST proteins have a&#xd;
signal peptide, indicating that these proteins enter the secretory pathway, and the mature proteins have tandem&#xd;
repeat oligopeptides that share a hexapeptide (E/D)FEPRP followed by 4 partially conserved amino acids, which&#xd;
could determine a putative N-glycosylation signal, and a fully conserved tyrosine. In a phylogenetic tree, the&#xd;
sequences clade according to taxonomic group. A possible involvement in symbiosis and abiotic stress as well as in&#xd;
plant cell elongation is suggested, although different STs could play different roles in plant development.&#xd;
Conclusions: We describe a new family of proteins called ST whose presence is limited to the plant kingdom,&#xd;
specifically to a few families of dicotyledonous plants. They present 20 to 40 amino acid tandem repeat sequences&#xd;
with different characteristics (signal peptide, DUF2775 domain, conservative repeat regions) from the described&#xd;
group of 20 to 40 amino acid tandem repeat proteins and also from known cell wall proteins with repeat&#xd;
sequences. Several putative roles in plant physiology can be inferred from the characteristics found.</mods:abstract>
<mods:language>
<mods:languageTerm>eng</mods:languageTerm>
</mods:language>
<mods:accessCondition type="useAndReproduction">http://creativecommons.org/licenses/by-nc-nd/4.0/</mods:accessCondition>
<mods:accessCondition type="useAndReproduction">info:eu-repo/semantics/embargoedAccess</mods:accessCondition>
<mods:accessCondition type="useAndReproduction">Attribution-NonCommercial-NoDerivatives 4.0 Internacional</mods:accessCondition>
<mods:subject>
<mods:topic>Biotic interaction</mods:topic>
</mods:subject>
<mods:subject>
<mods:topic>DUF2775 domain</mods:topic>
</mods:subject>
<mods:subject>
<mods:topic>ST proteins</mods:topic>
</mods:subject>
<mods:subject>
<mods:topic>Tandem repeat proteins</mods:topic>
</mods:subject>
<mods:titleInfo>
<mods:title>ST proteins, a new family of plant tandem repeat proteins with a DUF2775 domain mainly found in Fabaceae and Asteraceae</mods:title>
</mods:titleInfo>
<mods:genre>info:eu-repo/semantics/article</mods:genre>
</mods:mods></metadata></record></GetRecord></OAI-PMH>