Occurrence of a putative SCF ubiquitin ligase complex in Drosophila

Many proteins are targeted to proteasome degradation by a family of E3 ubiquitin ligases, termed SCF complexes, that link substrate proteins to an E2 ubiquitin-conjugating enzyme. SCFs are composed of three core proteins-Skp1, Cdc53/Cull, Rbx1/Hrt1-and a substrate specific F-box protein. We have ide...

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Detalles Bibliográficos
Autores principales:	Bocca, S.N., Muzzopappa, M., Silberstein, S., Wappner, P.
Formato:	JOUR
Materias:	Drosophila E3 ligase Proteolysis SCF Ubiquitin ligase proteasome ubiquitin article Drosophila melanogaster enzyme activity nonhuman nucleotide sequence polymerase chain reaction priority journal protein analysis protein degradation protein interaction protein purification Saccharomyces cerevisiae
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_0006291X_v286_n2_p357_Bocca
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_0006291X_v286_n2_p357_Bocca
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spelling	todo:paper_0006291X_v286_n2_p357_Bocca2023-10-03T14:03:48Z Occurrence of a putative SCF ubiquitin ligase complex in Drosophila Bocca, S.N. Muzzopappa, M. Silberstein, S. Wappner, P. Drosophila E3 ligase Proteolysis SCF Ubiquitin ligase proteasome ubiquitin article Drosophila Drosophila melanogaster enzyme activity nonhuman nucleotide sequence polymerase chain reaction priority journal protein analysis protein degradation protein interaction protein purification Saccharomyces cerevisiae Many proteins are targeted to proteasome degradation by a family of E3 ubiquitin ligases, termed SCF complexes, that link substrate proteins to an E2 ubiquitin-conjugating enzyme. SCFs are composed of three core proteins-Skp1, Cdc53/Cull, Rbx1/Hrt1-and a substrate specific F-box protein. We have identified in Drosophila melanogaster the closest homologues to the human components of the SCFβTrCP complex and the E2 ubiquitin-conjugating enzyme UbcH5. We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb. We also describe the direct interaction of the UbcH5 related protein UbcD1 with dCul1 and Slmb. In addition, a functional complementation test performed on a Saccharomyces cerevisiae Hrt1p-deficient mutant showed that Drosophila Rbx1 is able to restore the yeast cells viability. Our results suggest that dRbx1, dSkpA, dCullin1, and Slimb proteins are components of a Drosophila SCF complex that functions in combination with the ubiquitin conjugating enzyme UbcD1. © 2001 Academic Press. Fil:Bocca, S.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Muzzopappa, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Silberstein, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Wappner, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0006291X_v286_n2_p357_Bocca
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Drosophila E3 ligase Proteolysis SCF Ubiquitin ligase proteasome ubiquitin article Drosophila Drosophila melanogaster enzyme activity nonhuman nucleotide sequence polymerase chain reaction priority journal protein analysis protein degradation protein interaction protein purification Saccharomyces cerevisiae
spellingShingle	Drosophila E3 ligase Proteolysis SCF Ubiquitin ligase proteasome ubiquitin article Drosophila Drosophila melanogaster enzyme activity nonhuman nucleotide sequence polymerase chain reaction priority journal protein analysis protein degradation protein interaction protein purification Saccharomyces cerevisiae Bocca, S.N. Muzzopappa, M. Silberstein, S. Wappner, P. Occurrence of a putative SCF ubiquitin ligase complex in Drosophila
topic_facet	Drosophila E3 ligase Proteolysis SCF Ubiquitin ligase proteasome ubiquitin article Drosophila Drosophila melanogaster enzyme activity nonhuman nucleotide sequence polymerase chain reaction priority journal protein analysis protein degradation protein interaction protein purification Saccharomyces cerevisiae
description	Many proteins are targeted to proteasome degradation by a family of E3 ubiquitin ligases, termed SCF complexes, that link substrate proteins to an E2 ubiquitin-conjugating enzyme. SCFs are composed of three core proteins-Skp1, Cdc53/Cull, Rbx1/Hrt1-and a substrate specific F-box protein. We have identified in Drosophila melanogaster the closest homologues to the human components of the SCFβTrCP complex and the E2 ubiquitin-conjugating enzyme UbcH5. We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb. We also describe the direct interaction of the UbcH5 related protein UbcD1 with dCul1 and Slmb. In addition, a functional complementation test performed on a Saccharomyces cerevisiae Hrt1p-deficient mutant showed that Drosophila Rbx1 is able to restore the yeast cells viability. Our results suggest that dRbx1, dSkpA, dCullin1, and Slimb proteins are components of a Drosophila SCF complex that functions in combination with the ubiquitin conjugating enzyme UbcD1. © 2001 Academic Press.
format	JOUR
author	Bocca, S.N. Muzzopappa, M. Silberstein, S. Wappner, P.
author_facet	Bocca, S.N. Muzzopappa, M. Silberstein, S. Wappner, P.
author_sort	Bocca, S.N.
title	Occurrence of a putative SCF ubiquitin ligase complex in Drosophila
title_short	Occurrence of a putative SCF ubiquitin ligase complex in Drosophila
title_full	Occurrence of a putative SCF ubiquitin ligase complex in Drosophila
title_fullStr	Occurrence of a putative SCF ubiquitin ligase complex in Drosophila
title_full_unstemmed	Occurrence of a putative SCF ubiquitin ligase complex in Drosophila
title_sort	occurrence of a putative scf ubiquitin ligase complex in drosophila
url	http://hdl.handle.net/20.500.12110/paper_0006291X_v286_n2_p357_Bocca
work_keys_str_mv	AT boccasn occurrenceofaputativescfubiquitinligasecomplexindrosophila AT muzzopappam occurrenceofaputativescfubiquitinligasecomplexindrosophila AT silbersteins occurrenceofaputativescfubiquitinligasecomplexindrosophila AT wappnerp occurrenceofaputativescfubiquitinligasecomplexindrosophila
_version_	1782030172367618048

Occurrence of a putative SCF ubiquitin ligase complex in Drosophila

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