DOI: 10.1083/jcb.152.1.75. A Functional Interaction between the Survival Motor Neuron Complex and RNA Polymerase II [Penn]

A Functional Interaction between the Survival Motor Neuron Complex and RNA Polymerase II

10.1083/jcb.152.1.75

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

The survival motor neuron (SMN) protein, the protein product of the spinal muscular atrophy (SMA) disease gene, plays a role in the assembly and regeneration of small nuclear ribonucleoproteins (snRNPs) and spliceosomes. By nanoelectrospray mass spectrometry, we identified RNA helicase A (RHA) as an SMN complex–associated protein. RHA is a DEAH box RNA helicase which binds RNA polymerase II (pol II) and reportedly functions in transcription. SMN interacts with RHA in vitro, and this interaction is impaired in mutant SMNs found in SMA patients. Coimmunoprecipitation demonstrated that the SMN complex is associated with pol II, snRNPs, and RHA in vivo. In vitro experiments suggest that RHA mediates the association of SMN with the COOH-terminal domain of pol II. Moreover, transfection of cells with a dominant negative mutant of SMN, SMNΔN27, causes accumulation of pol II, snRNPs, and RHA in nuclear structures that contain the known markers of gems and coiled bodies, and inhibits RNA pol I and pol II transcription in vivo. These findings indicate a functional as well as physical association of the SMN complex with pol II and suggest a role for the SMN complex in the assembly of the pol II transcription/processing machinery.

Bibliography

Pellizzoni, L., Charroux, B., Rappsilber, J., Mann, M., & Dreyfuss, G. (2001). A Functional Interaction between the Survival Motor Neuron Complex and RNA Polymerase II. The Journal of Cell Biology, 152(1), 75â86.

Authors 5

Livio Pellizzoni (first)
Bernard Charroux (additional)
Juri Rappsilber (additional)
Matthias Mann (additional)
Gideon Dreyfuss (additional)

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Dates

Type	When
Created	23 years ago (July 26, 2002, 12:46 p.m.)
Deposited	2 years ago (July 28, 2023, 10:54 p.m.)
Indexed	3 days, 21 hours ago (Aug. 19, 2025, 7:05 a.m.)
Issued	24 years, 7 months ago (Jan. 8, 2001)
Published	24 years, 7 months ago (Jan. 8, 2001)
Published Online	24 years, 7 months ago (Jan. 8, 2001)
Published Print	24 years, 7 months ago (Jan. 8, 2001)

Funders 0

None

BibTeX

@article{Pellizzoni_2001, title={A Functional Interaction between the Survival Motor Neuron Complex and RNA Polymerase II}, volume={152}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.152.1.75}, DOI={10.1083/jcb.152.1.75}, number={1}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Pellizzoni, Livio and Charroux, Bernard and Rappsilber, Juri and Mann, Matthias and Dreyfuss, Gideon}, year={2001}, month=jan, pages={75–86} }

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  "abstract": "<jats:p>The survival motor neuron (SMN) protein, the protein product of the spinal muscular atrophy (SMA) disease gene, plays a role in the assembly and regeneration of small nuclear ribonucleoproteins (snRNPs) and spliceosomes. By nanoelectrospray mass spectrometry, we identified RNA helicase A (RHA) as an SMN complex\u2013associated protein. RHA is a DEAH box RNA helicase which binds RNA polymerase II (pol II) and reportedly functions in transcription. SMN interacts with RHA in vitro, and this interaction is impaired in mutant SMNs found in SMA patients. Coimmunoprecipitation demonstrated that the SMN complex is associated with pol II, snRNPs, and RHA in vivo. In vitro experiments suggest that RHA mediates the association of SMN with the COOH-terminal domain of pol II. Moreover, transfection of cells with a dominant negative mutant of SMN, SMN\u0394N27, causes accumulation of pol II, snRNPs, and RHA in nuclear structures that contain the known markers of gems and coiled bodies, and inhibits RNA pol I and pol II transcription in vivo. These findings indicate a functional as well as physical association of the SMN complex with pol II and suggest a role for the SMN complex in the assembly of the pol II transcription/processing machinery.</jats:p>",
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