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Updated: Sep 10, 2026

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
Published on: May 13, 2019
TRiC/CCT chaperonin governs RNA polymerase II activity in the nucleus to support RNA homeostasis
Zlata Gvozdenov1, Anusmita Biswas2, Audrey Yi Tyan Peng2
1Department of Cell and Developmental Biology, School of Molecular and Cellular Biology, University of Illinois-Urbana-Champaign, Urbana, IL 61801, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 94305, USA.
Abstract:
Eukaryotic tailless complex polypeptide 1 ring complex/Chaperonin containing tailless complex polypeptide 1 (TRiC/CCT) chaperonin is typically considered a cytosolic machine mediating polypeptide folding and assembly of protein complexes. Here, we investigated the nuclear role of TRiC/CCT. Use of a TRiC/CCT temperature-sensitive allele revealed increased production of nascent RNA leading to the accumulation of noncoding transcripts. TRiC/CCT was associated with RNA polymerase II (RNAPII) in vitro and in vivo, including when bound to DNA. Heat treatment of the TRiC/CCT ts chaperonin stabilized the RNAPII complex association and binding to the actin and tubulin substrates. Expression of the Huntingtin protein Htt correlated with lowered RNA production and a decreased association between the RNAPII and TRiC/CCT complexes. Together, our presented data support a model where TRiC/CCT regulates the global activity of RNAPII in reaction to the status of proteostasis. Overall, our work reveals an avenue by which TRiC/CCT contributes to homeostasis by regulating the activity of nuclear RNAPII.
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