Low Complexity Regions behave as tRNA sponges to help co-translational folding of plasmodial proteins

Autor: Elizabetta Pizzi, Manuel A. S. Santos, Anne Théobald-Dietrich, Maya Ayach, Joëlle Rudinger-Thirion, Magali Frugier, Tania Bour
Přispěvatelé: Architecture et Réactivité de l'ARN (ARN), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Department of Biology and CESAM, Universidade de Aveiro, Dipartimento di Malattie Infettive, Parassitarie ed Immunomediate, Istituto Superiore di Sanita [Rome]
Rok vydání: 2009
Předmět:
Protein Folding
Translational efficiency
MESH: Protein Folding
Protein domain
Molecular Sequence Data
Plasmodium falciparum
Biophysics
MESH: Protein Structure
Secondary
MESH: Amino Acid Sequence
Computational biology
Biology
Biochemistry
Ribosome
Protein Structure
Secondary
Amino Acyl-tRNA Synthetases
03 medical and health sciences
Protein structure
RNA
Transfer
Structural Biology
Genetics
Protein biosynthesis
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Amino Acid Sequence
RNA
Messenger
MESH: Amino Acyl-tRNA Synthetases
Co‐translational folding
Molecular Biology
MESH: Plasmodium falciparum
MESH: RNA
Messenger
030304 developmental biology
0303 health sciences
MESH: Molecular Sequence Data
030302 biochemistry & molecular biology
Translation (biology)
Cell Biology
MESH: RNA
Transfer
Molecular biology
3. Good health
Mutagenesis
Insertional
MESH: Mutagenesis
Insertional
Co-translational folding
MESH: Protein Biosynthesis
Protein Biosynthesis
Transfer RNA
Low complexity regions
Protein folding
MESH: Ribosomes
Ribosomes
Zdroj: FEBS Letters; Vol 584
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
FEBS Letters
FEBS Letters, Wiley, 2010, 584 (2), pp.448-54. ⟨10.1016/j.febslet.2009.11.004⟩
ISSN: 1873-3468
0014-5793
Popis: International audience; In most organisms, the information necessary to specify the native 3D-structures of proteins is encoded in the corresponding mRNA sequences. Translational accuracy and efficiency are coupled and sequences that are slowly translated play an essential role in the concomitant folding of protein domains. Here, we suggest that the well-known mechanisms for the regulation of translational efficiency, which involves mRNA structure and/or asymmetric tRNA abundance, do not apply to all organisms. We propose that Plasmodium, the parasite responsible for malaria, uses an alternative strategy to slow down ribosomal speed and avoid multidomain protein misfolding during translation. In our model, the abundant Low Complexity Regions present in Plasmodium proteins replace the codon preferences, which influence the assembly of protein secondary structures.
Databáze: OpenAIRE
Externí odkaz: