Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk

Ribosome-inactivating proteins (RIPs) inhibit protein synthesis by depurinating an adenine on the sarcin–ricin loop (SRL) of the large subunit ribosomal RNA. Several RIPs interact with the C-terminal end of ribosomal stalk P proteins, and this interaction is required for their full activity. In cont...

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Bibliographic Details
Published in:Toxicon (Oxford) 2012-03, Vol.59 (3), p.427-432
Main Authors: Lapadula, Walter J., Sanchez-Puerta, M. Virginia, Juri Ayub, Maximiliano
Format: Article
Language:English
Subjects:
adenine
Amino Acid Sequence
Animal poisons toxicology. Antivenoms
Bayes Theorem
Biological and medical sciences
convergent evolution
DNA-Binding Proteins - metabolism
Evolution, Molecular
Medical sciences
Models, Molecular
Molecular Sequence Data
Phylogeny
Phytolacca americana
Protein Biosynthesis
protein synthesis
proteins
ribosomal RNA
Ribosome inactivating protein
Ribosome Inactivating Proteins - metabolism
ribosomes
Ribosomes - genetics
Ribosomes - metabolism
Ricin - genetics
Ricin - metabolism
RNA, Ribosomal - genetics
RNA, Ribosomal - metabolism
Sequence Alignment
Stalk
Toxicology
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Summary:Ribosome-inactivating proteins (RIPs) inhibit protein synthesis by depurinating an adenine on the sarcin–ricin loop (SRL) of the large subunit ribosomal RNA. Several RIPs interact with the C-terminal end of ribosomal stalk P proteins, and this interaction is required for their full activity. In contrast, the activity of Pokeweed Antiviral Protein is not affected by blocking this stalk component. Here, we provide evidence from phylogenetic analyses and sequence alignments suggesting that the interaction with the C-terminal end of P proteins evolved independently in different RIPs by convergent evolution.
ISSN:0041-0101
1879-3150
DOI:10.1016/j.toxicon.2011.12.014