Proteomics

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An extended PAXT connection is required for turnover of nuclear polyadenylated RNA in human cells

ABSTRACT: Recruitment of the human ribonucleolytic RNA exosome to nuclear polyadenylated (pA+) RNA is facilitated by the Poly(A) Tail eXosome Targeting (PAXT) connection. Besides its core dimer, formed by the exosome co-factor MTR4 and the ZFC3H1 protein, the PAXT connection remains poorly defined. By characterizing nuclear pA+-RNA bound proteomes as well as MTR4-ZFC3H1 containing complexes in conditions favoring PAXT assembly, we here uncover three additional proteins required for PAXT function: ZC3H3, RBM26/RBM27 and the known PAXT-associated protein, PABPN1. The zinc-finger protein ZC3H3 interacts directly with MTR4-ZFC3H1 and loss of either identified PAXT component results in the accumulation of PAXT substrates. Collectively, our results establish new factors involved in the turnover of nuclear pA+ RNA and suggest that these are limiting for PAXT activity.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Torben Heick Jensen 

PROVIDER: PXD016070 | JPOST Repository | Thu Oct 31 00:00:00 GMT 2019

REPOSITORIES: jPOST

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The human ZC3H3 and RBM26/27 proteins are critical for PAXT-mediated nuclear RNA decay.

Silla Toomas T   Schmid Manfred M   Dou Yuhui Y   Garland William W   Milek Miha M   Imami Koshi K   Johnsen Dennis D   Polak Patrik P   Andersen Jens S JS   Selbach Matthias M   Landthaler Markus M   Jensen Torben Heick TH  

Nucleic acids research 20200301 5

Recruitment of the human ribonucleolytic RNA exosome to nuclear polyadenylated (pA+) RNA is facilitated by the Poly(A) Tail eXosome Targeting (PAXT) connection. Besides its core dimer, formed by the exosome co-factor MTR4 and the ZFC3H1 protein, the PAXT connection remains poorly defined. By characterizing nuclear pA+-RNA bound proteomes as well as MTR4-ZFC3H1 containing complexes in conditions favoring PAXT assembly, we here uncover three additional proteins required for PAXT function: ZC3H3, R  ...[more]

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