Actin and hnRNP U cooperate for productive transcription by RNA polymerase II

Alexander Kukalev, Ylva Nord, Carina Palmberg, Tomas Bergman, Piergiorgio Percipalle

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)238-244
Number of pages7
JournalNature Structural and Molecular Biology
Volume12
Issue number3
DOIs
StatePublished - Dec 1 2005

Fingerprint

Heterogeneous-Nuclear Ribonucleoprotein U
RNA Polymerase II
Actins
Microfilament Proteins
Ribonucleoproteins
Microinjections
RNA Interference
Affinity Chromatography
HeLa Cells
Transcriptional Activation
Amino Acid Sequence

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 journalArticle

Kukalev, Alexander ; Nord, Ylva ; Palmberg, Carina ; Bergman, Tomas ; Percipalle, Piergiorgio. / Actin and hnRNP U cooperate for productive transcription by RNA polymerase II. In: Nature Structural and Molecular Biology. 2005 ; Vol. 12, No. 3. pp. 238-244.
@article{5b0fdbbf1aba4959be7fd2579499ab43,
title = "Actin and hnRNP U cooperate for productive transcription by RNA polymerase II",
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.",
author = "Alexander Kukalev and Ylva Nord and Carina Palmberg and Tomas Bergman and Piergiorgio Percipalle",
year = "2005",
month = "12",
day = "1",
doi = "10.1038/nsmb904",
language = "English (US)",
volume = "12",
pages = "238--244",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "3",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=17844391563&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=17844391563&partnerID=8YFLogxK

U2 - 10.1038/nsmb904

DO - 10.1038/nsmb904

M3 - Article

C2 - 15711563

AN - SCOPUS:17844391563

VL - 12

SP - 238

EP - 244

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 3

ER -