Protein-protein interaction map of the Trypanosoma cruzi ribosomal P protein complex
The large subunit of the eukaryotic ribosome possesses a long and protruding stalk formed by the ribosomal P proteins. Four out of five ribosomal P proteins of Trypanosoma cruzi, TcP0, TcP1α, TcP2α, and TcP2β had been previously characterized. Data mining of the T. cruzi genome data base allowed the...
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todo:paper_03781119_v357_n2_p129_Ayub2023-10-03T15:31:49Z Protein-protein interaction map of the Trypanosoma cruzi ribosomal P protein complex Ayub, M.J. Smulski, C.R. Nyambega, B. Bercovich, N. Masiga, D. Vazquez, M.P. Aguilar, C.F. Levin, M.J. Protein-protein interaction Ribosomal P protein Ribosome Trypanosoma cruzi Yeast two-hybrid glycine cleavage system article complex formation dimerization evaluation nonhuman nucleotide sequence priority journal protein protein interaction quantitative analysis ribosome Trypanosoma cruzi Amino Acid Sequence Animals Dimerization Molecular Sequence Data Multiprotein Complexes Peptide Mapping Phosphoproteins Protein Binding Protozoan Proteins Ribosomal Proteins Trypanosoma cruzi Two-Hybrid System Techniques Eukaryota Trypanosoma cruzi The large subunit of the eukaryotic ribosome possesses a long and protruding stalk formed by the ribosomal P proteins. Four out of five ribosomal P proteins of Trypanosoma cruzi, TcP0, TcP1α, TcP2α, and TcP2β had been previously characterized. Data mining of the T. cruzi genome data base allowed the identification of the fifth member of this protein group, a novel P1 protein, named P1β. To gain insight into the assembly of the stalk, a yeast two-hybrid based protein interaction map was generated. A parasite specific profile of interactions amongst the ribosomal P proteins of T. cruzi was evident. The TcP0 protein was able to interact with all both P1 and both P2 proteins. Moreover, the interactions between P2β with P1α as well as with P2α were detected, as well as the ability of TcP2β to homodimerize. A quantitative evaluation of the interactions established that the strongest interacting pair was TcP0-TcP1β. © 2005 Elsevier B.V. All rights reserved. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03781119_v357_n2_p129_Ayub |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Protein-protein interaction Ribosomal P protein Ribosome Trypanosoma cruzi Yeast two-hybrid glycine cleavage system article complex formation dimerization evaluation nonhuman nucleotide sequence priority journal protein protein interaction quantitative analysis ribosome Trypanosoma cruzi Amino Acid Sequence Animals Dimerization Molecular Sequence Data Multiprotein Complexes Peptide Mapping Phosphoproteins Protein Binding Protozoan Proteins Ribosomal Proteins Trypanosoma cruzi Two-Hybrid System Techniques Eukaryota Trypanosoma cruzi |
spellingShingle |
Protein-protein interaction Ribosomal P protein Ribosome Trypanosoma cruzi Yeast two-hybrid glycine cleavage system article complex formation dimerization evaluation nonhuman nucleotide sequence priority journal protein protein interaction quantitative analysis ribosome Trypanosoma cruzi Amino Acid Sequence Animals Dimerization Molecular Sequence Data Multiprotein Complexes Peptide Mapping Phosphoproteins Protein Binding Protozoan Proteins Ribosomal Proteins Trypanosoma cruzi Two-Hybrid System Techniques Eukaryota Trypanosoma cruzi Ayub, M.J. Smulski, C.R. Nyambega, B. Bercovich, N. Masiga, D. Vazquez, M.P. Aguilar, C.F. Levin, M.J. Protein-protein interaction map of the Trypanosoma cruzi ribosomal P protein complex |
topic_facet |
Protein-protein interaction Ribosomal P protein Ribosome Trypanosoma cruzi Yeast two-hybrid glycine cleavage system article complex formation dimerization evaluation nonhuman nucleotide sequence priority journal protein protein interaction quantitative analysis ribosome Trypanosoma cruzi Amino Acid Sequence Animals Dimerization Molecular Sequence Data Multiprotein Complexes Peptide Mapping Phosphoproteins Protein Binding Protozoan Proteins Ribosomal Proteins Trypanosoma cruzi Two-Hybrid System Techniques Eukaryota Trypanosoma cruzi |
description |
The large subunit of the eukaryotic ribosome possesses a long and protruding stalk formed by the ribosomal P proteins. Four out of five ribosomal P proteins of Trypanosoma cruzi, TcP0, TcP1α, TcP2α, and TcP2β had been previously characterized. Data mining of the T. cruzi genome data base allowed the identification of the fifth member of this protein group, a novel P1 protein, named P1β. To gain insight into the assembly of the stalk, a yeast two-hybrid based protein interaction map was generated. A parasite specific profile of interactions amongst the ribosomal P proteins of T. cruzi was evident. The TcP0 protein was able to interact with all both P1 and both P2 proteins. Moreover, the interactions between P2β with P1α as well as with P2α were detected, as well as the ability of TcP2β to homodimerize. A quantitative evaluation of the interactions established that the strongest interacting pair was TcP0-TcP1β. © 2005 Elsevier B.V. All rights reserved. |
format |
JOUR |
author |
Ayub, M.J. Smulski, C.R. Nyambega, B. Bercovich, N. Masiga, D. Vazquez, M.P. Aguilar, C.F. Levin, M.J. |
author_facet |
Ayub, M.J. Smulski, C.R. Nyambega, B. Bercovich, N. Masiga, D. Vazquez, M.P. Aguilar, C.F. Levin, M.J. |
author_sort |
Ayub, M.J. |
title |
Protein-protein interaction map of the Trypanosoma cruzi ribosomal P protein complex |
title_short |
Protein-protein interaction map of the Trypanosoma cruzi ribosomal P protein complex |
title_full |
Protein-protein interaction map of the Trypanosoma cruzi ribosomal P protein complex |
title_fullStr |
Protein-protein interaction map of the Trypanosoma cruzi ribosomal P protein complex |
title_full_unstemmed |
Protein-protein interaction map of the Trypanosoma cruzi ribosomal P protein complex |
title_sort |
protein-protein interaction map of the trypanosoma cruzi ribosomal p protein complex |
url |
http://hdl.handle.net/20.500.12110/paper_03781119_v357_n2_p129_Ayub |
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