| Autor: |
Barros, Géssica C., Requião, Rodrigo D., Carneiro, Rodolfo L., Masuda, Claudio A., Moreira, Mariana H., Rossetto, Silvana, Domitrovic, Tatiana, Palhano, Fernando L. |
| Jazyk: |
angličtina |
| Rok vydání: |
2019 |
| DOI: |
10.1101/849851 |
| Popis: |
Highly positively charged protein segments are known to result in poor translation efficiency by the action of the ribosome quality control (RQC) complex. This effect may be explained by ribosome stalling caused by electrostatic interactions between the nascent peptide and the negatively charged ribosome exit tunnel, leading to translation termination followed by the protein degradation by the RQC complex. These polybasic peptides are mainly studied with reporter systems, where artificial sequences are introduced into heterologous genes. The unique example of an endogenous protein targeted by the RQC complex is Rqc1, a protein essential for RQC function. The polybasic motif in Rqc1 N-terminal is thought to activate the RQC, leading to Rqc1 down-regulation. We aimed to determine whether the RQC complex acts as a regulatory mechanism for other endogenous proteins containing polybasic segments. Here, we show by bioinformatics, ribosome profiling data, and western blot protein quantification that endogenous proteins containing polybasic motifs similar to or even more positively charged than Rqc1 are not targeted by the RQC complex, suggesting that endogenous polybasic motifs do not induce degradation by this complex. We further demonstrate that Rqc1 levels are not regulated by the RQC complex but by Ltn1 alone in a posttranslational fashion. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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