Abstract
To determine the role of actin-ribonucleoprotein complexes in transcription, we set out to identify novel actin-binding proteins associated with RNA polymerase II (Pol II). Using affinity chromatography on fractionated HeLa cells, we found that hnRNP U binds actin through a short amino acid sequence in its C-terminal domain. Post-transcriptional gene silencing of hnRNP U and nuclear microinjections of a short peptide encompassing the hnRNP U actin-binding sequence inhibited BrUTP incorporation in vivo. In living cells, we found that both actin and hnRNP U are associated with the phosphorylated C-terminal domain of Pol II, and antibodies to actin and hnRNP U blocked Pol II-mediated transcription. Taken together, our results indicate that a general actin-based mechanism is implicated in the transcription of most Pol II genes. Actin in complex with hnRNP U may carry out its regulatory role during the initial phases of transcription activation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 238-244 |
| Number of pages | 7 |
| Journal | Nature Structural and Molecular Biology |
| Volume | 12 |
| Issue number | 3 |
| DOIs | |
| State | Published - Dec 1 2005 |
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ASJC Scopus subject areas
- Molecular Biology
- Structural Biology
Cite this
Actin and hnRNP U cooperate for productive transcription by RNA polymerase II. / Kukalev, Alexander; Nord, Ylva; Palmberg, Carina; Bergman, Tomas; Percipalle, Piergiorgio.
In: Nature Structural and Molecular Biology, Vol. 12, No. 3, 01.12.2005, p. 238-244.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Actin and hnRNP U cooperate for productive transcription by RNA polymerase II
AU - Kukalev, Alexander
AU - Nord, Ylva
AU - Palmberg, Carina
AU - Bergman, Tomas
AU - Percipalle, Piergiorgio
PY - 2005/12/1
Y1 - 2005/12/1
N2 - To determine the role of actin-ribonucleoprotein complexes in transcription, we set out to identify novel actin-binding proteins associated with RNA polymerase II (Pol II). Using affinity chromatography on fractionated HeLa cells, we found that hnRNP U binds actin through a short amino acid sequence in its C-terminal domain. Post-transcriptional gene silencing of hnRNP U and nuclear microinjections of a short peptide encompassing the hnRNP U actin-binding sequence inhibited BrUTP incorporation in vivo. In living cells, we found that both actin and hnRNP U are associated with the phosphorylated C-terminal domain of Pol II, and antibodies to actin and hnRNP U blocked Pol II-mediated transcription. Taken together, our results indicate that a general actin-based mechanism is implicated in the transcription of most Pol II genes. Actin in complex with hnRNP U may carry out its regulatory role during the initial phases of transcription activation.
AB - To determine the role of actin-ribonucleoprotein complexes in transcription, we set out to identify novel actin-binding proteins associated with RNA polymerase II (Pol II). Using affinity chromatography on fractionated HeLa cells, we found that hnRNP U binds actin through a short amino acid sequence in its C-terminal domain. Post-transcriptional gene silencing of hnRNP U and nuclear microinjections of a short peptide encompassing the hnRNP U actin-binding sequence inhibited BrUTP incorporation in vivo. In living cells, we found that both actin and hnRNP U are associated with the phosphorylated C-terminal domain of Pol II, and antibodies to actin and hnRNP U blocked Pol II-mediated transcription. Taken together, our results indicate that a general actin-based mechanism is implicated in the transcription of most Pol II genes. Actin in complex with hnRNP U may carry out its regulatory role during the initial phases of transcription activation.
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U2 - 10.1038/nsmb904
DO - 10.1038/nsmb904
M3 - Article
VL - 12
SP - 238
EP - 244
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 3
ER -