dc.creator | DOMINGO JIMENEZ LOPEZ | |
dc.creator | LAURA AGUILAR HENONIN | |
dc.creator | JUAN MANUEL GONZALEZ PRIETO | |
dc.creator | Víctor Hugo Aguilar Hernández | |
dc.creator | PLINIO ANTONIO GUZMAN VILLATE | |
dc.date | 2018 | |
dc.date.accessioned | 2023-07-21T19:18:37Z | |
dc.date.available | 2023-07-21T19:18:37Z | |
dc.identifier | http://cicy.repositorioinstitucional.mx/jspui/handle/1003/1528 | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/7737088 | |
dc.description | RING ubiquitin E3 ligases enclose a RING domain for ubiquitin ligase activity and associated domains and/or conserved motifs outside the RING domain that collectively facilitate their classification and usually reveal some of key information related to mechanism of action. Here we describe a new family of E3 ligases that encodes a RING-H2 domain related in sequence to the ATL and BTL RING-H2 domains. This family, named CTL, encodes a motif designed as YEELL that expands 21 amino acids next to the RING-H2 domain that is present across most eukaryotic lineages. E3 ubiquitin ligase BIG BROTHER is a plant CTL that regulates organ size, and SUMO-targeted ubiquitin E3 ligase RNF111/ARKADIA is a vertebrate CTL. Basal animal and vertebrate, as well as fungi species, encode a single CTL gene that constraints the number of paralogs observed in vertebrates. Conversely, as previously described in ATL and BTL families in plants, CTL genes range from a single copy in green algae and 3 to 5 copies in basal species to 9 to 35 copies in angiosperms. Our analysis describes key structural features of a novel family of E3 ubiquitin ligases as an integral component of the set of core eukaryotic genes. | |
dc.format | application/pdf | |
dc.language | eng | |
dc.relation | info:eu-repo/semantics/datasetDOI/10.1371/journal.pone.0190969 | |
dc.relation | citation:Jiménez-López, D., Aguilar-Henonin, L., González-Prieto, J. M., Aguilar-Hernández, V., & Guzmán, P. (2018). CTLs, a new class of RING-H2 ubiquitin ligases uncovered by YEELL, a motif close to the RING domain that is present across eukaryotes. PloS one, 13(1), e0190969. | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.rights | http://creativecommons.org/licenses/by-nc-nd/4.0 | |
dc.source | PloS one, 13(1), e0190969, 2018 | |
dc.subject | info:eu-repo/classification/Autores/CTL PROTEIN | |
dc.subject | info:eu-repo/classification/Autores/PROTEIN | |
dc.subject | info:eu-repo/classification/Autores/UBIQUITIN PROTEIN LIGASE E3 | |
dc.subject | info:eu-repo/classification/Autores/UNCLASSIFIED DRUG | |
dc.subject | info:eu-repo/classification/Autores/ZINC FINGER PROTEIN | |
dc.subject | info:eu-repo/classification/Autores/UBIQUITIN PROTEIN LIGASE | |
dc.subject | info:eu-repo/classification/cti/2 | |
dc.subject | info:eu-repo/classification/cti/2 | |
dc.title | CTLs, a new class of RING-H2 ubiquitin ligases uncovered by YEELL, a motif close to the ring domain that is present across eukaryotes | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:eu-repo/semantics/submittedVersion | |