Expansion and diversification of BTL ring-H2 ubiquitin ligases in angiosperms: putative Rabring7/BCA2 orthologs.

RING finger E3 ligases are components of the ubiquitin proteasome system (UPS) that mediate the transfer of ubiquitin to substrates. Single-subunit RING finger E3s binds the E2 ubiquitin-conjugating enzyme and contains recognition sequences for the substrate within the same polypeptide. Here we desc...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Victor Aguilar-Hernández, Juliana Medina, Laura Aguilar-Henonin, Plinio Guzmán
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2013
Materias:
R
Q
Acceso en línea:https://doaj.org/article/712aa58bc2d64ce79454578a4fee97d6
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:712aa58bc2d64ce79454578a4fee97d6
record_format dspace
spelling oai:doaj.org-article:712aa58bc2d64ce79454578a4fee97d62021-11-18T09:00:31ZExpansion and diversification of BTL ring-H2 ubiquitin ligases in angiosperms: putative Rabring7/BCA2 orthologs.1932-620310.1371/journal.pone.0072729https://doaj.org/article/712aa58bc2d64ce79454578a4fee97d62013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23951330/?tool=EBIhttps://doaj.org/toc/1932-6203RING finger E3 ligases are components of the ubiquitin proteasome system (UPS) that mediate the transfer of ubiquitin to substrates. Single-subunit RING finger E3s binds the E2 ubiquitin-conjugating enzyme and contains recognition sequences for the substrate within the same polypeptide. Here we describe the characterization of a class of RING finger E3 ligases that is conserved among eukaryotes. This class encodes a RING-H2 domain related in sequence to the ATL RING-H2 domain, another class of E3 ligases, and a C2/C2 zing finger at the amino-terminus, formerly described as BZF. In viridiplantae (green algae and land plants), we designed this family as BTL for BZF ATLs. BTLs are putative orthologs of the mammalian Rabring7/BCA2 RING-H2 E3s that have expanded in angiosperms. They are found in numbers ranging from three to thirty-one, which is in contrast to the one to three members normally found in animals, fungi, and protists. Furthermore, the number of sequence LOGOs generated in angiosperms is four times greater than that in other eukaryotes. In contrast to ATLs, which show expansion by tandem duplication, tandemly duplicated BTLs are scarce. The mode of action of Rabring7/BCA2 and BTLs may be similar since both the Rabring7/BCA2 BZF and the ath|BTL4 BZF are likely to mediate the binding of ubiquitin. This study introduces valuable information on the evolution and domain structure of the Rabring7/BCA2/BTL class of E3 ligases which may be important for core eukaryotic genes.Victor Aguilar-HernándezJuliana MedinaLaura Aguilar-HenoninPlinio GuzmánPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 8, p e72729 (2013)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Victor Aguilar-Hernández
Juliana Medina
Laura Aguilar-Henonin
Plinio Guzmán
Expansion and diversification of BTL ring-H2 ubiquitin ligases in angiosperms: putative Rabring7/BCA2 orthologs.
description RING finger E3 ligases are components of the ubiquitin proteasome system (UPS) that mediate the transfer of ubiquitin to substrates. Single-subunit RING finger E3s binds the E2 ubiquitin-conjugating enzyme and contains recognition sequences for the substrate within the same polypeptide. Here we describe the characterization of a class of RING finger E3 ligases that is conserved among eukaryotes. This class encodes a RING-H2 domain related in sequence to the ATL RING-H2 domain, another class of E3 ligases, and a C2/C2 zing finger at the amino-terminus, formerly described as BZF. In viridiplantae (green algae and land plants), we designed this family as BTL for BZF ATLs. BTLs are putative orthologs of the mammalian Rabring7/BCA2 RING-H2 E3s that have expanded in angiosperms. They are found in numbers ranging from three to thirty-one, which is in contrast to the one to three members normally found in animals, fungi, and protists. Furthermore, the number of sequence LOGOs generated in angiosperms is four times greater than that in other eukaryotes. In contrast to ATLs, which show expansion by tandem duplication, tandemly duplicated BTLs are scarce. The mode of action of Rabring7/BCA2 and BTLs may be similar since both the Rabring7/BCA2 BZF and the ath|BTL4 BZF are likely to mediate the binding of ubiquitin. This study introduces valuable information on the evolution and domain structure of the Rabring7/BCA2/BTL class of E3 ligases which may be important for core eukaryotic genes.
format article
author Victor Aguilar-Hernández
Juliana Medina
Laura Aguilar-Henonin
Plinio Guzmán
author_facet Victor Aguilar-Hernández
Juliana Medina
Laura Aguilar-Henonin
Plinio Guzmán
author_sort Victor Aguilar-Hernández
title Expansion and diversification of BTL ring-H2 ubiquitin ligases in angiosperms: putative Rabring7/BCA2 orthologs.
title_short Expansion and diversification of BTL ring-H2 ubiquitin ligases in angiosperms: putative Rabring7/BCA2 orthologs.
title_full Expansion and diversification of BTL ring-H2 ubiquitin ligases in angiosperms: putative Rabring7/BCA2 orthologs.
title_fullStr Expansion and diversification of BTL ring-H2 ubiquitin ligases in angiosperms: putative Rabring7/BCA2 orthologs.
title_full_unstemmed Expansion and diversification of BTL ring-H2 ubiquitin ligases in angiosperms: putative Rabring7/BCA2 orthologs.
title_sort expansion and diversification of btl ring-h2 ubiquitin ligases in angiosperms: putative rabring7/bca2 orthologs.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/712aa58bc2d64ce79454578a4fee97d6
work_keys_str_mv AT victoraguilarhernandez expansionanddiversificationofbtlringh2ubiquitinligasesinangiospermsputativerabring7bca2orthologs
AT julianamedina expansionanddiversificationofbtlringh2ubiquitinligasesinangiospermsputativerabring7bca2orthologs
AT lauraaguilarhenonin expansionanddiversificationofbtlringh2ubiquitinligasesinangiospermsputativerabring7bca2orthologs
AT plinioguzman expansionanddiversificationofbtlringh2ubiquitinligasesinangiospermsputativerabring7bca2orthologs
_version_ 1718421027329933312