Nucleic Acids Research, 1995, Vol. 23, No. 20 4034-4041
© 1995
MOLECULAR BIOLOGY |
Isolation of genomic and cDNA clones encoding bovine poly(A) binding protein II
1Department of cell Biology, Universit
t Basel Klingelbergstrasse 70, CH-4056 Basel, Switzerland
2Department of Biochemistry, Universit
t Basel Klingelbergstrasse 70, CH-4056 Basel, Switzerland
3Department of Biophysics, Biozentrum Universit
t Basel Klingelbergstrasse 70, CH-4056 Basel, Switzerland
*To whom correspondence should be addressed
Received July 28, 1995. Revised September 14, 1995. Accepted September 14, 1995.
cDNA clones for bovine poly(A) binding protein II (PAB II) were isolated. Their sequence predicts a protein of 32.8 kDa, revising earlier estimates of molecular mass. The protein contains one putative RNA-binding domain of the RNP type, an acidic N-terminal and a basic C-terminal domain. Analyses of authentic PAB II were in good agreement with all predictions from the cDNA sequence except that a number of arginine residues appeared to be post-translationally modified. Poly(A) binding protein II expressed in Escherichia coli was active in poly(A) binding and reconstitution of processive polyadenylation, including poly(A) tail length control. The cDNA clones showed a number of potential PAB II binding sites in the 3' untranslated sequence. Bovine poly(A)+ RNA contained two mRNAs hybridizing to a PAB II-specific probe. Analysis of a genomic clone revealed six introns in the coding sequence. The revised molecular mass led to a demonstration of PAB II oligomer formation and a reinterpretation of earlier data concerning the protein's binding to poly(A).
+present address: Universität Giessen, Institut für Biochemie. Heinrich-Buff-Ring 58, D-35392 Giessen. Germany
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
U. Kuhn, M. Gundel, A. Knoth, Y. Kerwitz, S. Rudel, and E. Wahle Poly(A) Tail Length Is Controlled by the Nuclear Poly(A)-binding Protein Regulating the Interaction between Poly(A) Polymerase and the Cleavage and Polyadenylation Specificity Factor J. Biol. Chem., August 21, 2009; 284(34): 22803 - 22814. [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] |
||||
![]() |
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] |
||||
![]() |
A. Perreault, C. Lemieux, and F. Bachand Regulation of the Nuclear Poly(A)-binding Protein by Arginine Methylation in Fission Yeast J. Biol. Chem., March 9, 2007; 282(10): 7552 - 7562. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Hosoda, F. Lejeune, and L. E. Maquat Evidence that Poly(A) Binding Protein C1 Binds Nuclear Pre-mRNA Poly(A) Tails Mol. Cell. Biol., April 15, 2006; 26(8): 3085 - 3097. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. P. TAVANEZ, P. CALADO, J. BRAGA, M. LAFARGA, and M. CARMO-FONSECA In vivo aggregation properties of the nuclear poly(A)-binding protein PABPN1 RNA, May 1, 2005; 11(5): 752 - 762. [Abstract] [Full Text] [PDF] |
||||
![]() |
U. Kuhn, A. Nemeth, S. Meyer, and E. Wahle The RNA Binding Domains of the Nuclear poly(A)-binding Protein J. Biol. Chem., May 2, 2003; 278(19): 16916 - 16925. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Calapez, H. M. Pereira, A. Calado, J. Braga, J. Rino, C. Carvalho, J. P. Tavanez, E. Wahle, A. C. Rosa, and M. Carmo-Fonseca The intranuclear mobility of messenger RNA binding proteins is ATP dependent and temperature sensitive J. Cell Biol., December 9, 2002; 159(5): 795 - 805. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y. P. Bao, L. J. Cook, D. O'Donovan, E. Uyama, and D. C. Rubinsztein Mammalian, Yeast, Bacterial, and Chemical Chaperones Reduce Aggregate Formation and Death in a Cell Model of Oculopharyngeal Muscular Dystrophy J. Biol. Chem., March 29, 2002; 277(14): 12263 - 12269. [Abstract] [Full Text] [PDF] |
||||
![]() |
X. Fan, P. Dion, J. Laganiere, B. Brais, and G. A. Rouleau Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death Hum. Mol. Genet., October 1, 2001; 10(21): 2341 - 2351. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y.-J. Kim, S. Noguchi, Y. K. Hayashi, T. Tsukahara, T. Shimizu, and K. Arahata The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression Hum. Mol. Genet., May 1, 2001; 10(11): 1129 - 1139. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Calado, F. M.S. Tome, B. Brais, G.A. Rouleau, U. Kuhn, E. Wahle, and M. Carmo-Fonseca Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA Hum. Mol. Genet., September 1, 2000; 9(15): 2321 - 2328. [Abstract] [Full Text] [PDF] |
||||
![]() |
A Calado and M Carmo-Fonseca Localization of poly(A)-binding protein 2 (PABP2) in nuclear speckles is independent of import into the nucleus and requires binding to poly(A) RNA J. Cell Sci., January 6, 2000; 113(12): 2309 - 2318. [Abstract] [PDF] |
||||
![]() |
J. Zhao, L. Hyman, and C. Moore Formation of mRNA 3' Ends in Eukaryotes: Mechanism, Regulation, and Interrelationships with Other Steps in mRNA Synthesis Microbiol. Mol. Biol. Rev., June 1, 1999; 63(2): 405 - 445. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. J. Smith, K. P. Rucknagel, A. Schierhorn, J. Tang, A. Nemeth, M. Linder, H. R. Herschman, and E. Wahle Unusual Sites of Arginine Methylation in Poly(A)-binding Protein II and in Vitro Methylation by Protein Arginine Methyltransferases PRMT1 and PRMT3 J. Biol. Chem., May 7, 1999; 274(19): 13229 - 13234. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. M. Kessler, J. Zhao, and C. L. Moore Purification of the Saccharomyces cerevisiae Cleavage/Polyadenylation Factor I. SEPARATION INTO TWO COMPONENTS THAT ARE REQUIRED FOR BOTH CLEAVAGE AND POLYADENYLATION OF mRNA 3prime ENDS J. Biol. Chem., October 25, 1996; 271(43): 27167 - 27175. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. Lellek, R. Kirsten, I. Diehl, F. Apostel, F. Buck, and J. Greeve Purification and Molecular Cloning of a Novel Essential Component of the Apolipoprotein B mRNA Editing Enzyme-Complex J. Biol. Chem., June 23, 2000; 275(26): 19848 - 19856. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. Winstall, M. Sadowski, U. Kuhn, E. Wahle, and A. B. Sachs The Saccharomyces cerevisiae RNA-binding Protein Rbp29 Functions in Cytoplasmic mRNA Metabolism J. Biol. Chem., July 14, 2000; 275(29): 21817 - 21826. [Abstract] [Full Text] [PDF] |
||||






