riboswitch

It is the only riboswitch found so far in eukaryotes.

The structure of the lysine riboswitch has recently been determined.

Its relatively complex secondary structure could indicate that it is a riboswitch.

In other words, the response curve of the riboswitch better resembles a digital function.

The lysine riboswitch has also been identified independently and called the L box.

The S box riboswitch is found only in the order Lactobacillales.

In this regulation, the riboswitch interferes with transcription of the gene.

However, the scaffolds of these two types of riboswitch appear to be quite distinct.

These three varieties of riboswitch have no obvious similarities in terms of sequence or structure.

Variants of the riboswitch consensus have been identified.

The following riboswitch mechanisms have been experimentally demonstrated.

Geobacter uraniumreducens is predicted to have 30 instances of this riboswitch in its genome.

The 3-d structure of the tetrahydrofolate riboswitch has been solved by separate groups using X-ray crystallography.

Additionally, the fluoride riboswitch and the downstream regulated genes can be potential targets for drug development in the future.

This riboswitch is found in a number of genes involved in lysine metabolism, including lysC.

The original definition of the term "riboswitch" specified that they directly sense small-molecule metabolite concentrations.

A riboswitch in Listeria monocytogenes regulates the expression of its downstream gene.

Its is proposed to be a subclass of the previously described classical AdoCbl-sensing riboswitch.

The preQ riboswitch is distinguished by its unusually small aptamer, compared to other riboswitches.

This guiding research help characterize the fluoride riboswitch's own interactions with fluoride and its structure.

The crystal structure of the riboswitch from E. faecalis was solved by X-ray crystallography.

For example, a riboswitch can directly bind a small target molecule, the binding of the target affects the gene's activity.

The three dimensional structure of a fluoride riboswitch has been solved at atomic resolution by X-ray crystallography.

All known members of this riboswitch class appear to control members of COG4708 genes.

The x-ray crystal structure of the TPP riboswitch aptamer has been solved.