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Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

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Bacterial aptamers that selectively bind glutamine.

Tyler D Ames¹, Ronald R Breaker

¹Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT, USA.

|February 2, 2011

Summary

This summary is machine-generated.

Researchers discovered novel RNA motifs, glnA and Downstream-peptide, that bind L-glutamine. These findings suggest glutamine regulates nitrogen metabolism in cyanobacteria, expanding known amino acid aptamers.

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Published on: April 9, 2017

Area of Science:

Molecular Biology
Genomics
Biochemistry

Background:

Comparative sequence analysis reveals conserved RNA motifs.
Two structured non-coding RNA motifs, glnA and Downstream-peptide, show sequence and structural similarities.

Purpose of the Study:

To demonstrate that glnA and Downstream-peptide RNA motifs selectively bind L-glutamine.
To investigate the genomic distribution and potential regulatory function of these RNA motifs.

Main Methods:

Comparative sequence analysis of microbial data.
Experimental validation of L-glutamine binding to RNA motifs.
Analysis of genomic distribution and gene context.

Main Results:

Both glnA and Downstream-peptide RNA motifs selectively bind L-glutamine, acting as glutamine aptamers.
These aptamers are found in cyanobacteria and marine metagenomic sequences.
Several glnA RNA motifs are located upstream of nitrogen metabolism genes, suggesting a regulatory role.

Conclusions:

The identified RNA motifs are components of glutamine-responsive riboswitches.
Glutamine likely regulates nitrogen metabolism pathways in cyanobacteria.
This expands the known classes of natural amino acid aptamers to include glutamine, glycine, and lysine.