Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it (PubMed:19825635). Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (PubMed:19825635). Together with other chaperonins, contribute to the regulation of gene expression by modulating the spliceosome function on pre-mRNA splicing post-transcriptionally by acting as a co-chaperone of Hsp90 to control levels of LSM8 (PubMed:32396196). Required for microtubules (MTs) organization and dynamicity (By similarity). Involved in the process leading to microtubules dissociation in response to gibberellic acid (GA) probably due to the DELLA proteins-mediated translocation of the prefoldin co-chaperone complex from the cytoplasm to the nucleus (By similarity). Heterohexamer of two PFD-alpha type and four PFD-beta type subunits forming prefoldin co-chaperone complex (By similarity). Interacts with LSM8, a specific subunit of the LSM2-8 complex, which is a core component of the spliceosome (PubMed:32396196). In the presence of gibberellic acid (GA) and at room temperature, the prefoldin complex stays in the cytoplasm and is functional (By similarity). But in the absence of GA or in response to cold, the prefoldin complex is localized to the nucleus in the presence of DELLA proteins, which severely compromises alpha/beta-tubulin heterodimer availability, thus affecting microtubules (MTs) organization (By similarity). This changing subcellular localization follows a daily rhythm coordinated oscillation (By similarity). Accumulates in response to cold. Smaller plants (PubMed:32396196). Lower pre-mRNA splicing events and reduced production of U6 snRNA in plants lacking PFD2, PFD4 and PFD6, probably due to a reduced activity of the LSM2-8 complex (PubMed:32396196). Belongs to the prefoldin subunit beta family.