Involvement of Mitochondrial Ribosomal Proteins in Ribosomal RNA-mediated Protein Folding
| Autor: | Dibyendu Samanta, Anindita Das, Jaydip Ghosh, Debasis Das, Arpita Bhattacharya, Chanchal Das Gupta |
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| Rok vydání: | 2011 |
| Předmět: |
Protein Folding
Peptidyl transferase Molecular Sequence Data Mitochondria Liver Biology DNA Mitochondrial Biochemistry Ribosome Protein Structure Secondary 23S ribosomal RNA Ribosomal protein Escherichia coli Animals Humans Eukaryotic Small Ribosomal Subunit Amino Acid Sequence Molecular Biology 50S Leishmania Sequence Homology Amino Acid Eukaryotic Large Ribosomal Subunit Cell Biology Mitochondria Protein Structure Tertiary RNA Ribosomal Mutation biology.protein Nucleic Acid Conformation RNA Cattle lipids (amino acids peptides and proteins) Eukaryotic Ribosome Ribosomes Allosteric Site |
| Zdroj: | Journal of Biological Chemistry. 286:43771-43781 |
| ISSN: | 0021-9258 |
| Popis: | The peptidyl transferase center of the domain V of large ribosomal RNA in the prokaryotic and eukaryotic cytosolic ribosomes acts as general protein folding modulator. We showed earlier that one part of the domain V (RNA1 containing the peptidyl transferase loop) binds unfolded protein and directs it to a folding competent state (FCS) that is released by the other part (RNA2) to attain the folded native state by itself. Here we show that the peptidyl transferase loop of the mitochondrial ribosome releases unfolded proteins in FCS extremely slowly despite its lack of the rRNA segment analogous to RNA2. The release of FCS can be hastened by the equivalent activity of RNA2 or the large subunit proteins of the mitochondrial ribosome. The RNA2 or large subunit proteins probably introduce some allosteric change in the peptidyl transferase loop to enable it to release proteins in FCS. |
| Databáze: | OpenAIRE |
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