Artículo
SNRPD2 Is a Novel Substrate for the Ubiquitin Ligase Activity of the Salmonella Type III Secretion Effector SlrP
Autor/es | Bullones Bolaños, Andrea Simone
Araujo Garrido, Juan Luis Fernández García, Jesús Romero Portillo, Francisco Bernal Bayard, Joaquín Ramos Morales, Francisco |
Departamento | Universidad de Sevilla. Departamento de Genética Universidad de Sevilla. Departamento de Microbiología |
Fecha de publicación | 2022 |
Fecha de depósito | 2022-11-11 |
Publicado en |
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Resumen | SlrP is a protein with E3 ubiquitin ligase activity that is translocated by Salmonella enterica serovar Typhimurium into eukaryotic host cells through a type III secretion system. A yeast two-hybrid screen was performed ... SlrP is a protein with E3 ubiquitin ligase activity that is translocated by Salmonella enterica serovar Typhimurium into eukaryotic host cells through a type III secretion system. A yeast two-hybrid screen was performed to find new human partners for this protein. Among the interacting proteins identified by this screen was SNRPD2, a core component of the spliceosome. In vitro ubiquitination assays demonstrated that SNRPD2 is a substrate for the catalytic activity of SlrP, but not for other members of the NEL family of E3 ubiquitin ligases, SspH1 and SspH2. The lysine residues modified by this activity were identified by mass spectrometry. The identification of a new ubiquitination target for SlrP is a relevant contribution to the understanding of the role of this Salmonella effector. |
Agencias financiadoras | Ministerio de Ciencia e Innovación (MICIN). España Junta de Andalucía |
Identificador del proyecto | PID2019-106132RB-I00/AEI/10.13039/501100011033
P20_00576 US-1380805 |
Cita | Bullones Bolaños, A.S., Araujo Garrido, J.L., Fernández García, J., Romero Portillo, F., Bernal Bayard, J. y Ramos Morales, F. (2022). SNRPD2 Is a Novel Substrate for the Ubiquitin Ligase Activity of the Salmonella Type III Secretion Effector SlrP. Biology, 11 (10), 1517. https://doi.org/10.3390/biology11101517. |
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