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CTLs, a new class of RING-H2 ubiquitin ligases uncovered by YEELL, a motif close to the ring domain that is present across eukaryotes
DOMINGO JIMENEZ LOPEZ
LAURA AGUILAR HENONIN
JUAN MANUEL GONZALEZ PRIETO
Víctor Hugo Aguilar Hernández
PLINIO ANTONIO GUZMAN VILLATE
Acceso Abierto
Atribución-NoComercial-SinDerivadas
10.1371/journal.pone.0190969
CTL PROTEIN
PROTEIN
UBIQUITIN PROTEIN LIGASE E3
UNCLASSIFIED DRUG
ZINC FINGER PROTEIN
UBIQUITIN PROTEIN LIGASE
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.
2018
Artículo
PloS one, 13(1), e0190969, 2018
Inglés
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.
BIOLOGÍA Y QUÍMICA
Versión revisada
submittedVersion - Versión revisada
Aparece en las colecciones: Artículos de Investigación Arbitrados

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