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Pol II preferentially regulates ribosomal protein expression by trapping disassociated subunits

ABSTRACT: Pol II has been recognized as a passively regulated holoenzyme. However, whether Pol II plays specific regulatory roles remain unclear. Here, fractions containing disassociated RPB3 (dRPB3) were identified by size exclusion chromatography in various cells. Through a unique strategy, Specific Degradation of Disassociated Subunits (SDDS), we demonstrated that dRPB3 functions as a regulatory component of Pol II to enable the preferential control of 3’ end processing of ribosomal protein genes directly through its N-terminal domain. Machine learning analysis of large-scale genomic features revealed that the little elongation complex helps to specialize the functions of dRPB3. Mechanistically, dRPB3 facilitates CBC-PCF11 axis activity to increase the efficiency of 3’ end processing. Furthermore, RPB3 is dynamically regulated during development and diseases. These findings suggest that Pol II gains specific regulatory functions by trapping disassociated subunits.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: wenjia duan

LAB HEAD: Xiong Ji

PROVIDER: PXD038474 | Pride | 2023-02-14

REPOSITORIES: Pride

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			Action	DRS
	DWJ_20210318_Rpb3.raw	Raw
	DWJ_20210318_Rpb3_GG_M.xlsx	Xlsx
	checksum.txt	Txt

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