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Possible cooperation between eRF1 and suppressor tRNAs in stop codon reassigment in ciliates
Chai Baofeng 1 * #,Hao Yanrong 2,Xu Lijun 2,Li Cui 3,Shen Quan 2
1.Institute of Biotechnology, Shanxi University, Taiyuan 030006
2.Institute of Biotechnology, Shanxi University, Taiyuan, 030006
3.Faculty of Enviroment and Economics, Shanxi university of Financie and Economics, Taiyuan, 030006
*Correspondence author
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Funding: National Science Foundation of China （No.No.31172078; 30770294）, Fund for the Doctoral Program of Higher Education of China（No.20111401110008）
Opened online:21 January 2013
Accepted by: none
Citation: Chai Baofeng,Hao Yanrong,Xu Lijun.Possible cooperation between eRF1 and suppressor tRNAs in stop codon reassigment in ciliates[OL]. [21 January 2013] http://en.paper.edu.cn/en_releasepaper/content/4511917
 
 
One factor involved in eukaryotic translation termination is Class 1 release factor in eukaryotes (eRF1), which functions to decode stop codons. Variant code species, such as ciliates, frequently exhibit altered stop codon recognition. Studies revealed that some class-specific residues in the eRF1 N-terminal domain are responsible for stop codon reassignment in ciliates. Here, we investigated the effects on stop codon recognition of chimeric eRF1s containing the N-terminal domain of Euplotes octocarinatus and Blepharisma japonicum eRF1 fused to Saccharomyces cerevisiae M and C domains using dual luciferase read-through assays. Mutation of class-specific residues in different eRF1 classes was also studied to identify key residues and motifs involved in stop codon decoding. As expected, our results demonstrate that three pockets within the eRF1 N-terminal domain were involved in decoding stop codon nucleotides. However, allocation of residues to each pocket was revalued. Our data suggest that hydrophobic and class-specific surface residues participate in different functions: modulation of pocket conformation and interaction with stop codon nucleotides, respectively. Residues conserved across all eRF1s determine the relative orientation of the three pockets according to stop codon nucleotides. However, quantitative analysis of variant ciliate and yeast eRF1 point mutants did not reveal any correlation between evolutionary conservation of class-specific residues and termination-related functional specificity, and was limited in elucidating a detailed mechanism for ciliate stop codon reassignment. Thus, based on isolation of suppressor tRNAs from Euplotes and Tetrahymena, we propose that stop codon reassignment in ciliates may be controlled by cooperation between eRF1 and suppressor transfer RNAs
Keywords:eRF1; stop codon recognition; ciliates; suppressor tRNA
 
 
 

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