BC200 RNA is expressed in the dendrites as ribonucleoprotein particles. Protein synthesis at the synapses of neurons contribute to neuronal plasticity and help prevent neuronal degradation. Small, non-coding RNAs such as BC200 RNA work to repress translation by inhibiting its initiation. During eukaryotic translation, the preinitiation complex binds mRNA and scans the coding strand for a start codon. This step is often subject to the control of a family of initiation factors and these factors are often a target for translational regulators.  Poly(A)-binding protein (PABP) has been shown to bind to BC200 RNA further confirming their role as regulators of protein biosynthesis in synapses.
BC200 RNA targets an ATP-dependent RNA helicase called eukaryotic initiation factor 4A (eIF4A). eIF4A requires energy from ATP hydrolysis to unwind the double helix and initiate translation. However, BC200 RNA interferes with the transmission of energy after hydrolysis by changing the conformation of eIF4A, and thus the energy needed to unwind the double helix is never appropriately supplied and initiation of translation is inhibited.
This highly localized uncoupling of the ATPase activity, and subsequently the unwinding of the RNA duplex is proposed to have evolved as a result of the growing complexity of postsynaptic neurons and neuronal activities. Non-coding RNA molecules evolve at a much faster rate than gene-encoding proteins; thus, the sustained conservation of the BC200 RNA transcript indicates its importance for nervous system function.