Epstein-Barr Virus Nuclear Antigen 2 Binds via Its Methylated Arginine-Glycine Repeat to the Survival Motor Neuron Protein-Reference-Cited by-同舟云学术

Epstein-Barr Virus Nuclear Antigen 2 Binds via Its Methylated Arginine-Glycine Repeat to the Survival Motor Neuron Protein

Published:2003-04-15 Issue:8 Volume:77 Page:5008-5013
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:J Virol

Author:

Barth Stephanie¹,Liss Michael²,Voss Marc D.¹,Dobner Thomas²,Fischer Utz³,Meister Gunter³,Grässer Friedrich A.¹

Affiliation:

1. Institut für Medizinische Mikrobiologie und Hygiene, Abteilung Virologie, Universitätskliniken des Saarlandes, 66421 Homburg/Saar

2. Institut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum, 93053 Regensburg

3. Max Planck Institut für Biochemie, 82152 Martinsried/Munich, Germany

Abstract

ABSTRACT Here we provide evidence that EBNA2 is methylated in vivo and that methylation of EBNA2 is a prerequisite for binding to SMN. We present SMN as a novel binding partner of EBNA2 by showing that EBNA2 colocalizes with SMN in nuclear gems and that both proteins can be coimmunoprecipitated from cellular extract. Furthermore, in vitro methylation of either wild-type EBNA2 or a glutathione S -transferase-EBNA2 fusion protein encompassing the arginine-glycine (RG) repeat element is necessary for in vitro binding to the Tudor domain of SMN. The recently shown functional cooperation of SMN and EBNA2 in transcriptional activation and the previous observation of a severely reduced transformation potential yet strongly enhanced transcriptional activity of an EBNA2 mutant lacking the RG repeat indicate that binding of SMN to EBNA2 is a critical step in B-cell transformation by Epstein-Barr virus.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JVI.77.8.5008-5013.2003

Reference31 articles.

1. Bornkamm, G. W., and W. Hammerschmidt. 2001. Molecular virology of Epstein-Barr virus. Philos. Trans. R. Soc. Lond. B Biol. Sci. 356 : 437-459.

2. Brahms, H., L. Meheus, V. de Brabandere, U. Fischer, and R. Luhrmann. 2001. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA 7 : 1531-1542.

3. Branscombe, T. L., A. Frankel, J. H. Lee, J. R. Cook, Z. Yang, S. Pestka, and S. Clarke. 2001. PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. J. Biol. Chem. 276 : 32971-32976.

4. Campbell, L., C. M. D. Hunter, P. Mohagheg, J. M. Tinsley, M. A. Brasch, and K. E. Davies. 2000. Direct interaction of SMN with dp103, a putative RNA helicase: a role for SMN in transcription regulation? Hum. Mol. Genet. 9 : 1093-1100.

5. Charroux, B., L. Pellizzoni, R. A. Perkinson, A. Shevchenko, M. Mann, and G. Dreyfuss. 1999. Gemin3: a novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems. J. Cell Biol. 147 : 1181-1194.

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