HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 10, 7552-7562, March 9, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/10/7552    most recent M610512200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Perreault, A. Articles by Bachand, F. Search for Related Content PubMed PubMed Citation Articles by Perreault, A. Articles by Bachand, F. Social Bookmarking                      What's this?

Regulation of the Nuclear Poly(A)-binding Protein by Arginine Methylation in Fission Yeast^*

From the Department of Biochemistry, Université de Sherbrooke, Québec J1H 5N4, Canada

Two structurally different poly(A)-binding proteins (PABP) bind the poly(A) tract of mRNAs in most mammalian cells: PABPC in the cytoplasm and PABP2/PABPN1 in the nucleus. Whereas yeast orthologs of the cytoplasmic PABP are characterized, a gene product homologous to mammalian PABP2 has not been identified in yeast. We report here the identification of a homolog of PABP2 as an arginine methyltransferase 1 (RMT1)-associated protein in fission yeast. The product of the Schizosaccharomyces pombe pab2 gene encodes a nonessential nuclear protein and demonstrates specific poly(A) binding in vitro. Consistent with a functional role in poly(A) tail metabolism, mRNAs from pab2-null cells displayed hyperadenylated 3'-ends. We also show that arginine residues within the C-terminal arginine-rich domain of Pab2 are modified by RMT1-dependent methylation. Whereas the arginine methylated and unmethylated forms of Pab2 behaved similarly in terms of subcellular localization, poly(A) binding, and poly(A) tail length control; Pab2 oligomerization levels were markedly increased when Pab2 was not methylated. Significantly, Pab2 overexpression reduced growth rate, and this growth inhibitory effect was exacerbated in rmt1-null cells. Our results indicate that the main cellular function of Pab2 is in poly(A) tail length control and support a biological role for arginine methylation in the regulation of Pab2 oligomerization.

Received for publication, November 13, 2006 , and in revised form, January 9, 2007.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work.

² A Chercheur-Boursier of the Fonds de la Recherche en Santé du Québec (FRSQ). To whom correspondence should be addressed. Fax: 819-564-5340; E-mail: f.bachand{at}usherbrooke.ca.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				C. Lemieux and F. Bachand Cotranscriptional recruitment of the nuclear poly(A)-binding protein Pab2 to nascent transcripts and association with translating mRNPs Nucleic Acids Res., June 1, 2009; 37(10): 3418 - 3430. [Abstract] [Full Text] [PDF]

				A. Perreault, S. Gascon, A. D'Amours, J. M. Aletta, and F. Bachand A Methyltransferase-independent Function for Rmt3 in Ribosomal Subunit Homeostasis J. Biol. Chem., May 29, 2009; 284(22): 15026 - 15037. [Abstract] [Full Text] [PDF]

				J. A. Hurt, R. A. Obar, B. Zhai, N. G. Farny, S. P. Gygi, and P. A. Silver A conserved CCCH-type zinc finger protein regulates mRNA nuclear adenylation and export J. Cell Biol., April 20, 2009; 185(2): 265 - 277. [Abstract] [Full Text] [PDF]

				K. Kolbel, C. Ihling, K. Bellmann-Sickert, I. Neundorf, A. G. Beck-Sickinger, A. Sinz, U. Kuhn, and E. Wahle Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively J. Biol. Chem., March 27, 2009; 284(13): 8274 - 8282. [Abstract] [Full Text] [PDF]

				A. Perreault, C. Bellemer, and F. Bachand Nuclear export competence of pre-40S subunits in fission yeast requires the ribosomal protein Rps2 Nucleic Acids Res., November 1, 2008; 36(19): 6132 - 6142. [Abstract] [Full Text] [PDF]

				K. Fronz, S. Otto, K. Kolbel, U. Kuhn, H. Friedrich, A. Schierhorn, A. G. Beck-Sickinger, A. Ostareck-Lederer, and E. Wahle Promiscuous Modification of the Nuclear Poly(A)-binding Protein by Multiple Protein-arginine Methyltransferases Does Not Affect the Aggregation Behavior J. Biol. Chem., July 18, 2008; 283(29): 20408 - 20420. [Abstract] [Full Text] [PDF]

				N. Viphakone, F. Voisinet-Hakil, and L. Minvielle-Sebastia Molecular dissection of mRNA poly(A) tail length control in yeast Nucleic Acids Res., April 1, 2008; 36(7): 2418 - 2433. [Abstract] [Full Text] [PDF]

				D. A. Pasternack, J. Sayegh, S. Clarke, and L. K. Read Evolutionarily Divergent Type II Protein Arginine Methyltransferase in Trypanosoma brucei Eukaryot. Cell, September 1, 2007; 6(9): 1665 - 1681. [Abstract] [Full Text] [PDF]

				A. E. McBride, C. Zurita-Lopez, A. Regis, E. Blum, A. Conboy, S. Elf, and S. Clarke Protein Arginine Methylation in Candida albicans: Role in Nuclear Transport Eukaryot. Cell, July 1, 2007; 6(7): 1119 - 1129. [Abstract] [Full Text] [PDF]

				F. Bachand Protein Arginine Methyltransferases: from Unicellular Eukaryotes to Humans Eukaryot. Cell, June 1, 2007; 6(6): 889 - 898. [Full Text] [PDF]