Preliminary structural studies of the hydrophobic ribosomal P0 protein from Trypanosoma cruzi, a part of the P0/P1/P2 complex
The Trypanosoma cruzi ribosomal P0 protein (TcP0) is part of the ribosomal stalk, which is an elongated lateral protuberance of the large ribosomal subunit involved in the translocation step of protein synthesis. The TcP0 C-terminal peptide is highly antigenic and a major target of the antibody resp...
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2005
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09298665_v12_n6_p521_Ayub http://hdl.handle.net/20.500.12110/paper_09298665_v12_n6_p521_Ayub |
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paper:paper_09298665_v12_n6_p521_Ayub2023-06-08T15:52:25Z Preliminary structural studies of the hydrophobic ribosomal P0 protein from Trypanosoma cruzi, a part of the P0/P1/P2 complex Ribosomal P0 protein Structural Studies Trypanosoma cruzi multiprotein complex phosphoprotein phosphoprotein P0 recombinant protein ribosome protein amino acid sequence animal article chemistry circular dichroism genetics hydrophobicity metabolism molecular genetics protein binding protein secondary structure Trypanosoma cruzi Amino Acid Sequence Animals Circular Dichroism Hydrophobicity Molecular Sequence Data Multiprotein Complexes Phosphoproteins Protein Binding Protein Structure, Secondary Recombinant Proteins Ribosomal Proteins Trypanosoma cruzi Trypanosoma cruzi The Trypanosoma cruzi ribosomal P0 protein (TcP0) is part of the ribosomal stalk, which is an elongated lateral protuberance of the large ribosomal subunit involved in the translocation step of protein synthesis. The TcP0 C-terminal peptide is highly antigenic and a major target of the antibody response in patients with systemic lupus erythematosus and patients suffering chronic heart disease produced by Trypanosoma cruzi infection. The structural properties of TcP0 have been explored by circular dichroism, tryptophan fluorescence and limited proteolysis experiments. These studies were complemented by secondary structure consensus prediction analysis. The results suggest that the tertiary structure of TcP0 could be described as a compact, stable, trypsin-resistant, 200 residues long N-terminal domain belonging to the α/β class and a more flexible, degradable, helical, 123 residues long C-terminal domain which could be involved in the formation of an unusual hydrophobic zipper with the ribosomal P1/P2 proteins to form the P0/P1/P2 complex. © 2005 Bentham Science Publishers Ltd. 2005 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09298665_v12_n6_p521_Ayub http://hdl.handle.net/20.500.12110/paper_09298665_v12_n6_p521_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 |
Ribosomal P0 protein Structural Studies Trypanosoma cruzi multiprotein complex phosphoprotein phosphoprotein P0 recombinant protein ribosome protein amino acid sequence animal article chemistry circular dichroism genetics hydrophobicity metabolism molecular genetics protein binding protein secondary structure Trypanosoma cruzi Amino Acid Sequence Animals Circular Dichroism Hydrophobicity Molecular Sequence Data Multiprotein Complexes Phosphoproteins Protein Binding Protein Structure, Secondary Recombinant Proteins Ribosomal Proteins Trypanosoma cruzi Trypanosoma cruzi |
| spellingShingle |
Ribosomal P0 protein Structural Studies Trypanosoma cruzi multiprotein complex phosphoprotein phosphoprotein P0 recombinant protein ribosome protein amino acid sequence animal article chemistry circular dichroism genetics hydrophobicity metabolism molecular genetics protein binding protein secondary structure Trypanosoma cruzi Amino Acid Sequence Animals Circular Dichroism Hydrophobicity Molecular Sequence Data Multiprotein Complexes Phosphoproteins Protein Binding Protein Structure, Secondary Recombinant Proteins Ribosomal Proteins Trypanosoma cruzi Trypanosoma cruzi Preliminary structural studies of the hydrophobic ribosomal P0 protein from Trypanosoma cruzi, a part of the P0/P1/P2 complex |
| topic_facet |
Ribosomal P0 protein Structural Studies Trypanosoma cruzi multiprotein complex phosphoprotein phosphoprotein P0 recombinant protein ribosome protein amino acid sequence animal article chemistry circular dichroism genetics hydrophobicity metabolism molecular genetics protein binding protein secondary structure Trypanosoma cruzi Amino Acid Sequence Animals Circular Dichroism Hydrophobicity Molecular Sequence Data Multiprotein Complexes Phosphoproteins Protein Binding Protein Structure, Secondary Recombinant Proteins Ribosomal Proteins Trypanosoma cruzi Trypanosoma cruzi |
| description |
The Trypanosoma cruzi ribosomal P0 protein (TcP0) is part of the ribosomal stalk, which is an elongated lateral protuberance of the large ribosomal subunit involved in the translocation step of protein synthesis. The TcP0 C-terminal peptide is highly antigenic and a major target of the antibody response in patients with systemic lupus erythematosus and patients suffering chronic heart disease produced by Trypanosoma cruzi infection. The structural properties of TcP0 have been explored by circular dichroism, tryptophan fluorescence and limited proteolysis experiments. These studies were complemented by secondary structure consensus prediction analysis. The results suggest that the tertiary structure of TcP0 could be described as a compact, stable, trypsin-resistant, 200 residues long N-terminal domain belonging to the α/β class and a more flexible, degradable, helical, 123 residues long C-terminal domain which could be involved in the formation of an unusual hydrophobic zipper with the ribosomal P1/P2 proteins to form the P0/P1/P2 complex. © 2005 Bentham Science Publishers Ltd. |
| title |
Preliminary structural studies of the hydrophobic ribosomal P0 protein from Trypanosoma cruzi, a part of the P0/P1/P2 complex |
| title_short |
Preliminary structural studies of the hydrophobic ribosomal P0 protein from Trypanosoma cruzi, a part of the P0/P1/P2 complex |
| title_full |
Preliminary structural studies of the hydrophobic ribosomal P0 protein from Trypanosoma cruzi, a part of the P0/P1/P2 complex |
| title_fullStr |
Preliminary structural studies of the hydrophobic ribosomal P0 protein from Trypanosoma cruzi, a part of the P0/P1/P2 complex |
| title_full_unstemmed |
Preliminary structural studies of the hydrophobic ribosomal P0 protein from Trypanosoma cruzi, a part of the P0/P1/P2 complex |
| title_sort |
preliminary structural studies of the hydrophobic ribosomal p0 protein from trypanosoma cruzi, a part of the p0/p1/p2 complex |
| publishDate |
2005 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09298665_v12_n6_p521_Ayub http://hdl.handle.net/20.500.12110/paper_09298665_v12_n6_p521_Ayub |
| _version_ |
1768542795978506240 |