PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function

Jobert, Laure; Argentini, Manuela; Tora, Laszlo

doi:10.1016/J.YEXCR.2008.12.008

Title: PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function

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Abstract

TAF15 (formerly TAF{sub II}68) is a nuclear RNA-binding protein that is associated with a distinct population of TFIID and RNA polymerase II complexes. TAF15 harbours an N-terminal activation domain, an RNA recognition motif (RRM) and many Arg-Gly-Gly (RGG) repeats at its C-terminal end. The N-terminus of TAF15 serves as an essential transforming domain in the fusion oncoprotein created by chromosomal translocation in certain human chondrosarcomas. Post-transcriptional modifications (PTMs) of proteins are known to regulate their activity, however, nothing is known on how PTMs affect TAF15 function. Here we demonstrate that endogenous human TAF15 is methylated in vivo at its numerous RGG repeats. Furthermore, we identify protein arginine N-methyltransferase 1 (PRMT1) as a TAF15 interactor and the major PRMT responsible for its methylation. In addition, the RGG repeat-containing C-terminus of TAF15 is responsible for the shuttling between the nucleus and the cytoplasm and the methylation of RGG repeats affects the subcellular localization of TAF15. The methylation of TAF15 by PRMT1 is required for the ability of TAF15 to positively regulate the expression of the studied endogenous TAF15-target genes. Our findings demonstrate that arginine methylation of TAF15 by PRMT1 is a crucial event determining its proper localization and gene regulatory function.

Authors:

Jobert, Laure; Argentini, Manuela ^[1]; Tora, Laszlo ^[1]

Institut de Genetique et de Biologie Moleculaire et Cellulaire (IGBMC), CNRS UMR 7104, INSERM U 596, Universite Louis Pasteur de Strasbourg, BP 10142 - 67404 Illkirch Cedex, CU de Strasbourg (France)

Publication Date:: Wed Apr 15 00:00:00 EDT 2009

OSTI Identifier:: 22209815

Resource Type:: Journal Article

Journal Name:: Experimental Cell Research

Additional Journal Information:: Journal Volume: 315; Journal Issue: 7; Other Information: Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0014-4827

Country of Publication:: United States

Language:: English

Subject:: 60 APPLIED LIFE SCIENCES; ARGININE; CYTOPLASM; IN VIVO; METHYL TRANSFERASES; METHYLATION; RNA; SARCOMAS; SKELETAL DISEASES; TRANSCRIPTION; TRANSLOCATION

Citation Formats


                    Jobert, Laure, Argentini, Manuela, and Tora, Laszlo. PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function.  United States: N. p., 2009. 
        Web.  doi:10.1016/J.YEXCR.2008.12.008.

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                    Jobert, Laure, Argentini, Manuela, & Tora, Laszlo. PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function.  United States.  https://doi.org/10.1016/J.YEXCR.2008.12.008

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                    Jobert, Laure, Argentini, Manuela, and Tora, Laszlo. 2009.  
        "PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function".  United States.  https://doi.org/10.1016/J.YEXCR.2008.12.008.

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@article{osti_22209815,

  title        = {PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function},

  author       = {Jobert, Laure and Argentini, Manuela and Tora, Laszlo},

  abstractNote = {TAF15 (formerly TAF{sub II}68) is a nuclear RNA-binding protein that is associated with a distinct population of TFIID and RNA polymerase II complexes. TAF15 harbours an N-terminal activation domain, an RNA recognition motif (RRM) and many Arg-Gly-Gly (RGG) repeats at its C-terminal end. The N-terminus of TAF15 serves as an essential transforming domain in the fusion oncoprotein created by chromosomal translocation in certain human chondrosarcomas. Post-transcriptional modifications (PTMs) of proteins are known to regulate their activity, however, nothing is known on how PTMs affect TAF15 function. Here we demonstrate that endogenous human TAF15 is methylated in vivo at its numerous RGG repeats. Furthermore, we identify protein arginine N-methyltransferase 1 (PRMT1) as a TAF15 interactor and the major PRMT responsible for its methylation. In addition, the RGG repeat-containing C-terminus of TAF15 is responsible for the shuttling between the nucleus and the cytoplasm and the methylation of RGG repeats affects the subcellular localization of TAF15. The methylation of TAF15 by PRMT1 is required for the ability of TAF15 to positively regulate the expression of the studied endogenous TAF15-target genes. Our findings demonstrate that arginine methylation of TAF15 by PRMT1 is a crucial event determining its proper localization and gene regulatory function.},

  doi          = {10.1016/J.YEXCR.2008.12.008},

  url          = {https://www.osti.gov/biblio/22209815},
  journal      = {Experimental Cell Research},

  issn         = {0014-4827},

  number       = 7,

  volume       = 315,

  place        = {United States},

  year         = {Wed Apr 15 00:00:00 EDT 2009},

  month        = {Wed Apr 15 00:00:00 EDT 2009}

}

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