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Polyadenylate-binding protein, cytoplasmic and nuclear

 
Known also as: Poly(A)-binding protein, ARS consensus-binding protein ACBP-67, Polyadenylate tail-binding protein

Known abbreviations: PABP, PAB1, YER165W

 

FUNCTION:
 
Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, interacts with the nuclear cleavage factor IA (CFIA), which is required for both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. Regulates PAN activity via interaction with the stimulator PAN3 or the inhibitor PBP1. In the cytoplasm, affects both translation and mRNA decay. Stimulates translation by interaction with translation initiation factor eIF4G, a subunit of the cap-binding complex eIF4F, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. Also regulates translation termination by recruiting eukaryotic release factor 3 (eRF3). Interaction with eRF3 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN. Loss of PAB1 from the mRNP after deadenylation triggers mRNA degradation. Inhibits the major cytoplasmic mRNA deadenylase CCR4-NOT complex. Is also associated peripherally with COPI vesicles through its interaction with ARF1, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA. 
 
SUBUNIT STRUCTURE:
 
Binds to poly(A) mRNA to form a periodic structure with a packing density of one molecule per 25 adenylate residues. Interacts with the nuclear export factor CRM1 and with the importin SXM1. Interacts with RNA15, a component of the cleavage factor IA (CFIA) complex. Interacts with translation initiation factor eIF4G (TIF4631 or TIF4632) and release factor eRF3 (SUP35). Interacts with the PAB-dependent poly(A)-nuclease (PAN) complex regulatory subunit PAN3. Interacts with ARF1, DCP1, PBP1, the Hsp70 chaperone SSA1, and TPA1. Interacts with PAT1 in a RNA-dependent manner. 
 
CELLULAR LOCALIZATION:
 
Cytoplasm. Nucleus. Note: Predominantly cytoplasmic. Rapidly shuttles between the nucleus and the cytoplasm. Can be exported from the nucleus through at least 2 distinct pathways, the main being dependent on the exportin CRM1, and the second requiring MEX67 and ongoing mRNA export. Import is mediated by the importin SXM1. 
 
DOMAIN:
 
RNA recognition motifs (RRMs) 1 and 2 bind specifically to the poly(A) tail, whereas RRMs 3 and 4 bind non-specifically to polypyrimidine RNAs and may serve to bind to a different part of the messenger or to other RNAs. RRM 2 also mediates interaction with eIF-4G.



Activities in which Polyadenylate-binding protein, cytoplasmic and nuclear is involved: Pathways in which Polyadenylate-binding protein, cytoplasmic and nuclear is involved:

NCBI GI number(s): 6321013
296144337
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P04147 P04147
BRENDA - -
KEGG sce:YER165W sce:YER165W
PFAM: PF00658
PF00076
PF00658
PF00076
InterPro: IPR012677
IPR006515
IPR002004
IPR000504
IPR012677
IPR006515
IPR002004
IPR000504
CATH: - -
SCOP: - -
Solved crystal structures: 1IFW
[PDB] [details]


Protein sequence:
MADITDKTAEQLENLNIQDDQKQAATGSESQSVENSSASLYVGDLEPSVS
EAHLYDIFSPIGSVSSIRVCRDAITKTSLGYAYVNFNDHEAGRKAIEQLN
YTPIKGRLCRIMWSQRDPSLRKKGSGNIFIKNLHPDIDNKALYDTFSVFG
DILSSKIATDENGKSKGFGFVHFEEEGAAKEAIDALNGMLLNGQEIYVAP
HLSRKERDSQLEETKAHYTNLYVKNINSETTDEQFQELFAKFGPIVSASL
EKDADGKLKGFGFVNYEKHEDAVKAVEALNDSELNGEKLYVGRAQKKNER
MHVLKKQYEAYRLEKMAKYQGVNLFVKNLDDSVDDEKLEEEFAPYGTITS
AKVMRTENGKSKGFGFVCFSTPEEATKAITEKNQQIVAGKPLYVAIAQRK
DVRRSQLAQQIQARNQMRYQQATAAAAAAAAGMPGQFMPPMFYGVMPPRG
VPFNGPNPQQMNPMGGMPKNGMPPQFRNGPVYGVPPQGGFPRNANDNNQF
YQQKQRQALGEQLYKKVSAKTSNEEAAGKITGMILDLPPQEVFPLLESDE
LFEQHYKEASAAYESFKKEQEQQTEQA

Polyadenylate-binding protein, cytoplasmic and nuclear (Saccharomyces cerevisiae) is product of expression of PAB1 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae. Tucker M, Staples RR, Valencia-Sanchez MA, Muhlrad D, Parker R EMBO J 2002-03-15 (21) 11889048
Positive and negative regulation of poly(A) nuclease. Mangus DA, Evans MC, Agrin NS, Smith M, Gongidi P, Jacobson A Mol Cell Biol 2004-06-01 (24) 15169912
Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex recruited by Pab1, connect mRNA biogenesis to export. Dunn EF, Hammell CM, Hodge CA, Cole CN Genes Dev 2005-02-01 (19) 15630021
Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation. Hosoda N, Kobayashi T, Uchida N, Funakoshi Y, Kikuchi Y, Hoshino S, Katada T J Biol Chem 2003-10-03 (278) 12923185
The nucleotide sequence of Saccharomyces cerevisiae chromosome V. Dietrich FS, Mulligan J, Hennessy K, Yelton MA, Allen E, Araujo R, Aviles E, Berno A, Brennan T, Carpenter J, Chen E, Cherry JM, Chung E, Duncan M, Guzman E, Hartzell G, Hunicke-Smith S, Hyman RW, Kayser A, Komp C, Lashkari D, Lew H, Lin D, Mosedale D, Davis RW, et al. Nature 1997-05-01 (387) 9169868
Differential effects of aromatic and charged residue substitutions in the RNA binding domains of the yeast poly(A)-binding protein. Deardorff JA, Sachs AB J Mol Biol 1997-05-01 (269) 9193001
Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae. Hu Y, Rolfs A, Bhullar B, Murthy TV, Zhu C, Berger MF, Camargo AA, Kelley F, McCarron S, Jepson D, Richardson A, Raphael J, Moreira D, Taycher E, Zuo D, Mohr S, Kane MF, Williamson J, Simpson A, Bulyk ML, Harlow E, Marsischky G, Kolodner RD, LaBaer J Genome Res 2007-04-01 (17) 17322287
Global analysis of protein expression in yeast. Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O'Shea EK, Weissman JS Nature 2003-10-16 (425) 14562106
A multidimensional chromatography technology for in-depth phosphoproteome analysis. Albuquerque CP, Smolka MB, Payne SH, Bafna V, Eng J, Zhou H Mol Cell Proteomics 2008-07-01 (7) 18407956
Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation. Cosson B, Couturier A, Chabelskaya S, Kiktev D, Inge-Vechtomov S, Philippe M, Zhouravleva G Mol Cell Biol 2002-05-01 (22) 11971964
The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay. Kobayashi T, Funakoshi Y, Hoshino S, Katada T J Biol Chem 2004-10-01 (279) 15337765
A faux 3'-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay. Amrani N, Ganesan R, Kervestin S, Mangus DA, Ghosh S, Jacobson A Nature 2004-11-04 (432) 15525991
Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae. Keeling KM, Salas-Marco J, Osherovich LZ, Bedwell DM Mol Cell Biol 2006-07-01 (26) 16809762
A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression. Sachs AB, Bond MW, Kornberg RD Cell 1986-06-20 (45) 3518950
mRNA polyadenylate-binding protein: gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence. Adam SA, Nakagawa T, Swanson MS, Woodruff TK, Dreyfuss G Mol Cell Biol 1986-08-01 (6) 3537727
The yeast protein encoded by PUB1 binds T-rich single stranded DNA. Cockell M, Frutiger S, Hughes GJ, Gasser SM Nucleic Acids Res 1994-02-11 (22) 8127652
A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability. Sachs AB, Davis RW, Kornberg RD Mol Cell Biol 1987-09-01 (7) 3313012
The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation. Sachs AB, Davis RW Cell 1989-09-08 (58) 2673535
The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro. Bernstein P, Peltz SW, Ross J Mol Cell Biol 1989-01-01 (9) 2565532
The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Burd CG, Matunis EL, Dreyfuss G Mol Cell Biol 1991-07-01 (11) 1675426
PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae. Anderson JT, Paddy MR, Swanson MS Mol Cell Biol 1993-10-01 (13) 8413212
Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast. Caponigro G, Parker R Genes Dev 1995-10-01 (9) 7557393
Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G. Tarun SZ Jr, Sachs AB EMBO J 1996-12-16 (15) 9003792
Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins. Garrels JI, McLaughlin CS, Warner JR, Futcher B, Latter GI, Kobayashi R, Schwender B, Volpe T, Anderson DS, Mesquita-Fuentes R, Payne WE Electrophoresis 1997-08-01 (18) 9298649
Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro. Amrani N, Minet M, Le Gouar M, Lacroute F, Wyers F Mol Cell Biol 1997-07-01 (17) 9199303
The major yeast poly(A)-binding protein is associated with cleavage factor IA and functions in premessenger RNA 3'-end formation. Minvielle-Sebastia L, Preker PJ, Wiederkehr T, Strahm Y, Keller W Proc Natl Acad Sci U S A 1997-07-22 (94) 9223284
Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Tarun SZ Jr, Wells SE, Deardorff JA, Sachs AB Proc Natl Acad Sci U S A 1997-08-19 (94) 9256432
mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation. Coller JM, Gray NK, Wickens MP Genes Dev 1998-10-15 (12) 9784497
Circularization of mRNA by eukaryotic translation initiation factors. Wells SE, Hillner PE, Vale RD, Sachs AB Mol Cell 1998-07-01 (2) 9702200
RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G. Kessler SH, Sachs AB Mol Cell Biol 1998-02-01 (18) 9418852
Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation. Mangus DA, Amrani N, Jacobson A Mol Cell Biol 1998-12-01 (18) 9819425
The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms. Otero LJ, Ashe MP, Sachs AB EMBO J 1999-06-01 (18) 10357826
The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex. Vilela C, Velasco C, Ptushkina M, McCarthy JE EMBO J 2000-08-15 (19) 10944120
The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes. Horton LE, James P, Craig EA, Hensold JO J Biol Chem 2001-04-27 (276) 11279042
Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Tharun S, Parker R Mol Cell 2001-11-01 (8) 11741542
Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae. Trautwein M, Dengjel J, Schirle M, Spang A Mol Biol Cell 2004-11-01 (15) 15356266
Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export. Brune C, Munchel SE, Fischer N, Podtelejnikov AV, Weis K RNA 2005-04-01 (11) 15769879
Solution structure of the orphan PABC domain from Saccharomyces cerevisiae poly(A)-binding protein. Kozlov G, Siddiqui N, Coillet-Matillon S, Trempe JF, Ekiel I, Sprules T, Gehring K J Biol Chem 2002-06-21 (277) 11940585



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Last modification of this entry: Sept. 25, 2012.

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