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Domains two and three of Escherichia coli ribosomal S1 protein confers 30S subunits a high affinity for downstream A/U-rich mRNAs
- Source :
- The Journal of Biochemistry.
- Publication Year :
- 2019
- Publisher :
- Oxford University Press (OUP), 2019.
-
Abstract
- S1, a multi-domain ribosomal protein associated with the 30S subunit, is essential for translation initiation. S1 binds with high affinity to single-stranded mRNA containing A/U-rich patches upstream of the start codon. It was previously reported that domains 1-3 of S1 protein play a role in the docking and unfolding of structured mRNAs to the ribosome. Moreover, S1-deficient 30S subunits are still able to bind to low structured mRNAs. However, mRNAs containing A/U-rich patches in the early base positions after start codon enhance protein synthesis and mRNA binding to the ribosome, which suggests that S1 is also able to interact with these A/U-rich regions. To evaluate the essentiality of S1 domains in the binding to low structured mRNAs containing A/U/G nucleotides after the start codon as well as their role in translation and cell viability, S1 protein deletion variants were generated. We show that S1 domain 3 is necessary to discriminate these mRNAs according to the nucleotide nature since its absence abrogated S1 binding to A/U-rich mRNAs and allowed binding to G-rich mRNAs. Interestingly, domains 2 and 3 were required for the binding of mRNAs containing A/U-rich sequences after the start codon to 30S, in vitro translation and cell viability.
- Subjects :
- Ribosomal Proteins
Protein subunit
Ribosome Subunits, Small, Bacterial
Biochemistry
Ribosome
03 medical and health sciences
Eukaryotic translation
Protein Domains
Start codon
Ribosomal protein
Escherichia coli
Animals
30S
RNA, Messenger
Rats, Wistar
Molecular Biology
030304 developmental biology
0303 health sciences
Messenger RNA
Chemistry
030302 biochemistry & molecular biology
General Medicine
Ribosomal RNA
Rats
Cell biology
Female
Subjects
Details
- ISSN :
- 17562651 and 0021924X
- Database :
- OpenAIRE
- Journal :
- The Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....19717cb49108009f16f8cba3a71e2d8c