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...
Guardado en:
Autores principales: | , , , |
---|---|
Publicado: |
2001
|
Materias: | |
Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v286_n2_p357_Bocca http://hdl.handle.net/20.500.12110/paper_0006291X_v286_n2_p357_Bocca |
Aporte de: |
id |
paper:paper_0006291X_v286_n2_p357_Bocca |
---|---|
record_format |
dspace |
spelling |
paper:paper_0006291X_v286_n2_p357_Bocca2023-06-08T14:30:13Z Occurrence of a putative SCF ubiquitin ligase complex in Drosophila Bocca, Silvia N. Muzzopappa, Mariana Silberstein Cuña, Susana Iris Wappner, Pablo 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. 2001 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v286_n2_p357_Bocca 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, Silvia N. Muzzopappa, Mariana Silberstein Cuña, Susana Iris Wappner, Pablo 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. |
author |
Bocca, Silvia N. Muzzopappa, Mariana Silberstein Cuña, Susana Iris Wappner, Pablo |
author_facet |
Bocca, Silvia N. Muzzopappa, Mariana Silberstein Cuña, Susana Iris Wappner, Pablo |
author_sort |
Bocca, Silvia 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 |
publishDate |
2001 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v286_n2_p357_Bocca http://hdl.handle.net/20.500.12110/paper_0006291X_v286_n2_p357_Bocca |
work_keys_str_mv |
AT boccasilvian occurrenceofaputativescfubiquitinligasecomplexindrosophila AT muzzopappamariana occurrenceofaputativescfubiquitinligasecomplexindrosophila AT silbersteincunasusanairis occurrenceofaputativescfubiquitinligasecomplexindrosophila AT wappnerpablo occurrenceofaputativescfubiquitinligasecomplexindrosophila |
_version_ |
1768544619802394624 |