Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II

@article{Hofmann2004ActinIP,
  title={Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II},
  author={Wilma A. Hofmann and Ljuba Stojiljkovi{\'c} and Beata Fuchsov{\'a} and Gabriela M. Vargas and Evangelos Mavrommatis and Vlada V. Philimonenko and Katar{\'i}na Kysel{\'a} and James A. Goodrich and James L. Lessard and Thomas J. Hope and Pavel Hoz{\'a}k and Primal de Lanerolle},
  journal={Nature Cell Biology},
  year={2004},
  volume={6},
  pages={1094-1101}
}
Actin is abundant in the nucleus and has been implicated in transcription; however, the nature of this involvement has not been established. Here we demonstrate that β-actin is critically involved in transcription because antibodies directed against β-actin, but not muscle actin, inhibited transcription in vivo and in vitro. Chromatin immunoprecipitation assays demonstrated the recruitment of actin to the promoter region of the interferon-γ-inducible MHC2TA gene as well as the interferon… 

RNA helicase A acts as a bridging factor linking nuclear beta-actin with RNA polymerase II.

It is suggested that RHA acts as a bridging factor linking nuclear beta-actin with Pol II in PICs, and overexpression or depletion of RHA could influence the interaction of Pol II with beta- actin and beta-Actin-involved gene transcription regulation.

The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation

It is speculated that cofilin-1 performs its function in pol II transcription by regulating polymerization of gene-associated actin, facilitating association of elongating pol II and actin with active genes.

The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation.

It is speculated that cofilin-1 performs its function in pol II transcription by regulating polymerization of gene-associated actin, facilitating association of elongating pol II and actin with active genes.

A Novel Role of the Actin-nucleating Arp2/3 Complex in the Regulation of RNA Polymerase II-dependent Transcription*

Evidence is presented to show that the Arp2/3 complex is also localized in the nucleus and plays an essential role in mediating nuclear actin polymerization induced by N-WASP, and physically associates with RNA polymerase II and is involved in the RNA polymerases II-dependent transcriptional regulation both in vivo and in vitro.

Molecular functions of nuclear actin in transcription

A general model for actin in RNA polymerase II transcription is discussed whereby actin works as a conformational switch in conjunction with specific adaptors to facilitate the remodeling of large macromolecular assemblies at the promoter and along the active gene.

Actin and myosin in transcriptional and post-transcriptional control of gene expression

This thesis elucidates some of the molecular mechanisms through which nuclear actin controls synthesis and processing of RNA transcripts and proposes that NM1 accompanies newly assembled export-competent ribosomal subunits from nucleolus to NPC, thus modulating both their maturation and export.

Actin in transcription. Actin is required for transcription by all three RNA polymerases in the eukaryotic cell nucleus.

Evidence has emerged in recent years supporting the direct functional involvement of actin, and of nuclear myosin 1 (NM1), in transcription, both in insects and mammals, and probably in all eukaryotes.

Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its nuclear-binding partners

It is demonstrated that the interaction of N-WASP with the PSF–NonO complex can couple N-wasp with RNA polymerase II to regulate transcription, and proposed a nuclear function for N- WASP in transcriptional regulation is proposed.

G-actin Participates in RNA Polymerase II-dependent Transcription Elongation by Recruiting Positive Transcription Elongation Factor b (P-TEFb)*

The results suggested that actin participates in transcription elongation by recruiting Cdk9 for phosphorylation of the Pol II C-terminal domain, and the actin-Cdk9 interaction promotes chromatin remodeling.

Nuclear actin and myosin I are required for RNA polymerase I transcription

Investigation of the role of actin and nuclear myosin I in the transcription of ribosomal RNA genes (rDNA) suggests a role for NMI in the growth-dependent regulation of rRNA synthesis.
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