Although much previous research has focused on the role of IDP LC domains on intracellular condensation, RNA may be just as important due to its anionic backbone, which could affect valency-dependent interactions with peptides or proteins. Indeed, a number of RNA-binding proteins (RBPs) phase separate in the cell upon binding with RNA, leading to membraneless organelles called ribonucleoprotein (RNP) condensates formed through a combination of hydrophobic interactions, hydrogen bonds, and electrostatic interactions. The RNA-to-protein ratio is the key parameter for RNP assembly/disassembly, as low and high ratios tune up and down phase separation propensity, respectively. In fact, RNA drives the phase separation process of certain reentrant transitions, while RNA and RBPs are generally enriched in most membraneless nuclear bodies, suggesting that RNA and RBPs likely play a role in gene-regulatory functions of membraneless organelles. Numerous studies have revealed that inherent RNA characteristics are important in RNA-dependent condensates. For example, generation of stress granules is preferentially influenced by relatively lengthy transcripts with low levels of or no translation. In addition, RNA with complex secondary (or higher) structure can modulate protein aggregates to interact with proteins more frequently. N6methyladenosine modifications on RNA were even found to serve as a multivalent scaffold for the binding of YTHDF proteins, leading to phase separation. Nuclear RNA concentration itself even governs RBP solubility by acting as a buffer! These above-mentioned parameters of RNA collectively impart unique biophysical qualities in condensates, which are necessary for condensate functions in homeostasis and are inherently encoded in RNA.