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Structure of cytoplasmic RNA polymerase II

ABSTRACT: Before RNA polymerase II (Pol II) can enter the nucleus, where it transcribes messenger RNA, it must first be assembled in the cytoplasm. We have performed proteomic and structural analysis of endogenous human cytoplasmic Pol II complexes, enriched in known biogenesis factors including RPAP2 and the essential small GTPases, GPN1, and GPN3. Cryo-EM analysis revealed a structure of Pol II bound to RPAP2 and Gdown1 at a nominal resolution of 2.7 Å, in which previously unresolved regions of Gdown1 could be modeled. Analysis of reconstituted complexes revealed the interactions responsible for Pol II-RPAP2 association with GPN1 and GPN3, as well as how GPN1 and GPN3 form an intricate assembly together with RPAP2, whose stability is affected by GTP hydrolysis state. These combined revealed a network of interactions that chaperone Pol II in the cytoplasm and allow recycling of critical biogenesis complexes, and suggest a general model for how GPN-loop GTPases function.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Benjamin Neuditschko

LAB HEAD: Franz Herzog

PROVIDER: PXD070852 | Pride | 2026-07-14

REPOSITORIES: Pride

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			Action	DRS
	Pol_II_BS3-1_1.raw	Raw
	Pol_II_BS3-1_2.raw	Raw
	Pol_II_BS3.xls	Xls
	Pol_II_BS3_0_1.raw	Raw
	Pol_II_BS3_0_2.raw	Raw

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