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Updated: Feb 7, 2026
11:37
Simultaneous DNA-RNA Extraction from Coastal Sediments and Quantification of 16S rRNA Genes and Transcripts by Real-time PCR
Published on: June 11, 2016
18.4K
Evidence that 16S RNA from E. coli can assume two different biologically active conformations
Nucleic Acids Research
|August 1, 1976
Summary
Acetic acid-urea extracted 16S ribosomal RNA (rRNA) binds more ribosomal proteins due to its more open conformation. This structural difference, affecting protein binding and RNase susceptibility, is lost upon cold storage.
Area of Science:
- Molecular Biology
- Biochemistry
- Ribosome Biogenesis
Background:
- Ribosomal RNA (rRNA) conformation influences protein binding.
- Previous studies showed differences in protein binding capacity between extracted 16S rRNA types.
Purpose of the Study:
- To investigate the conformational differences between acetic acid-urea extracted and phenol extracted 16S rRNA.
- To correlate these conformational differences with protein binding capacity.
Main Methods:
- Acetic acid-urea precipitation for 16S rRNA extraction.
- Limited T1-RNase digestion assays.
- Electrophoretic mobility analysis.
- Protein binding assays.
Main Results:
- Acetic acid-urea extracted 16S rRNA exhibits a more "open" conformation compared to phenol extracted 16S rRNA.
- Acetic acid-urea 16S rRNA shows increased susceptibility to T1-RNase digestion.
- Acetic acid-urea 16S rRNA demonstrates slower electrophoretic mobility.
- Storage at -70°C leads to loss of conformational differences and reduced protein binding capacity for acetic acid-urea 16S rRNA.
Conclusions:
- The extraction method significantly impacts 16S rRNA conformation and protein binding.
- Conformational flexibility of 16S rRNA is crucial for its interaction with ribosomal proteins.
- Cold storage can alter rRNA structure and function, impacting ribosome assembly studies.
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