Preliminary Structural Studies of the Hydrophobic Ribosomal P0 Protein from Trypanosoma cruzi, A Part of the P0/P1/P2 Complex

Title: Preliminary Structural Studies of the Hydrophobic Ribosomal P0 Protein from Trypanosoma cruzi, A Part of the P0/P1/P2 Complex

Volume: 12 Issue: 6

Author(s): Maximiliano J. Ayub, Juan A. Barroso, Mariano J. Levin and Carlos F. Aguilar

Affiliation:

Keywords: trypanosoma cruzi, ribosomal po protein, structural studies

Abstract: 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 Cterminal 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.

Cite this article as:

Ayub J. Maximiliano, Barroso A. Juan, Levin J. Mariano and Aguilar F. Carlos, Preliminary Structural Studies of the Hydrophobic Ribosomal P0 Protein from Trypanosoma cruzi, A Part of the P0/P1/P2 Complex, Protein & Peptide Letters 2005; 12 (6) . https://dx.doi.org/10.2174/0929866054395879