Diversity in the Architecture of ATLs, a Family of Plant Ubiquitin-Ligases, Leads to Recognition and Targeting of Substrates in Different Cellular Environments
Identifieur interne : 000E11 ( Ncbi/Checkpoint ); précédent : 000E10; suivant : 000E12Diversity in the Architecture of ATLs, a Family of Plant Ubiquitin-Ligases, Leads to Recognition and Targeting of Substrates in Different Cellular Environments
Auteurs : Victor Aguilar-Hernández ; Laura Aguilar-Henonin ; Plinio GuzmánSource :
- PLoS ONE [ 1932-6203 ] ; 2011.
Abstract
Ubiquitin-ligases or E3s are components of the ubiquitin proteasome system (UPS) that coordinate the transfer of ubiquitin to the target protein. A major class of ubiquitin-ligases consists of RING-finger domain proteins that include the substrate recognition sequences in the same polypeptide; these are known as single-subunit RING finger E3s. We are studying a particular family of RING finger E3s, named ATL, that contain a transmembrane domain and the RING-H2 finger domain; none of the member of the family contains any other previously described domain. Although the study of a few members in
Url:
DOI: 10.1371/journal.pone.0023934
PubMed: 21887349
PubMed Central: 3161093
Affiliations:
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<author><name sortKey="Aguilar Henonin, Laura" sort="Aguilar Henonin, Laura" uniqKey="Aguilar Henonin L" first="Laura" last="Aguilar-Henonin">Laura Aguilar-Henonin</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Diversity in the Architecture of ATLs, a Family of Plant Ubiquitin-Ligases, Leads to Recognition and Targeting of Substrates in Different Cellular Environments</title>
<author><name sortKey="Aguilar Hernandez, Victor" sort="Aguilar Hernandez, Victor" uniqKey="Aguilar Hernandez V" first="Victor" last="Aguilar-Hernández">Victor Aguilar-Hernández</name>
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<author><name sortKey="Aguilar Henonin, Laura" sort="Aguilar Henonin, Laura" uniqKey="Aguilar Henonin L" first="Laura" last="Aguilar-Henonin">Laura Aguilar-Henonin</name>
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<author><name sortKey="Guzman, Plinio" sort="Guzman, Plinio" uniqKey="Guzman P" first="Plinio" last="Guzmán">Plinio Guzmán</name>
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<front><div type="abstract" xml:lang="en"><p>Ubiquitin-ligases or E3s are components of the ubiquitin proteasome system (UPS) that coordinate the transfer of ubiquitin to the target protein. A major class of ubiquitin-ligases consists of RING-finger domain proteins that include the substrate recognition sequences in the same polypeptide; these are known as single-subunit RING finger E3s. We are studying a particular family of RING finger E3s, named ATL, that contain a transmembrane domain and the RING-H2 finger domain; none of the member of the family contains any other previously described domain. Although the study of a few members in <italic>A. thaliana</italic>
and <italic>O. sativa</italic>
has been reported, the role of this family in the life cycle of a plant is still vague. To provide tools to advance on the functional analysis of this family we have undertaken a phylogenetic analysis of ATLs in twenty-four plant genomes. <italic>ATL</italic>
s were found in all the 24 plant species analyzed, in numbers ranging from 20–28 in two basal species to 162 in soybean. Analysis of <italic>ATL</italic>
s arrayed in tandem indicates that sets of genes are expanding in a species-specific manner. To get insights into the domain architecture of ATLs we generated 75 pHMM LOGOs from 1815 ATLs, and unraveled potential protein-protein interaction regions by means of yeast two-hybrid assays. Several ATLs were found to interact with DSK2a/ubiquilin through a region at the amino-terminal end, suggesting that this is a widespread interaction that may assist in the mode of action of ATLs; the region was traced to a distinct sequence LOGO. Our analysis provides significant observations on the evolution and expansion of the ATL family in addition to information on the domain structure of this class of ubiquitin-ligases that may be involved in plant adaptation to environmental stress.</p>
</div>
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