The aptamers were originally thought to cooperatively bind glycine to regulate the expression of downstream genes.

In Bacillus subtilis, this riboswitch is found upstream of the gcvT operon which controls glycine degradation.

[1] The originally discovered, truncated version of the glycine riboswitch exhibits sigmoidal binding curves with Hill coefficients greater than one, which led to the idea of positive cooperativity between the two aptamer domains.

[3] Atomic resolution structures of portions of glycine riboswitches have been obtained by X-ray crystallography.

Glycine-induced expression of the gcvT operon is needed for B. subtilise growth, swarming motility and biofilm formation (in high glycine environment).