Nuclear poly(A)-binding protein PABPN1 is associated with RNA polymerase II during transcription and accompanies the released transcript to the nuclear pore

被引:41
作者
Bear, DG
Fomproix, N
Soop, T
Björkroth, B
Masich, S
Daneholt, B
机构
[1] Univ New Mexico, Hlth Sci Ctr, Dept Cell Biol & Physiol, Albuquerque, NM 87131 USA
[2] Univ New Mexico, Hlth Sci Ctr, UNM Canc Res & Treatment Ctr, Albuquerque, NM 87131 USA
[3] Karolinska Inst, Dept Cell & Mol Biol, Med Nobel Inst, SE-17177 Stockholm, Sweden
基金
美国国家科学基金会;
关键词
PABPN1; PABP2; ribonucleoprotein; polyadenylation; mRNA trafficking; OPMD; cryo-immunoelectron microscopy;
D O I
10.1016/S0014-4827(03)00123-X
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
The nuclear poly(A)-binding protein, PABPN1, has been previously shown to regulate mRNA poly(A) tail length and to interact with selected proteins involved in mRNA synthesis and trafficking. To further understand the role of PABPN1 in mRNA metabolism, we used cryo-immunoelectron microscopy to determine the fate of PABPN1 at various stages in the assembly and transport of the Chironomus tentans salivary gland Balbiand ring (BR) mRNA ribonucleoprotein (mRNP) complex. PABPN1 is found on BR mRNPs within the nucleoplasm as well as on mRNPs docked at the nuclear pore. Very little PABPN1 is detected on the cytoplasmic side of the nuclear envelope, suggesting that PABPN1 is displaced from mRNPs during or shortly after passage through the nuclear pore. Surprisingly, we also find PABPN1 associated with RNA polymerase 11 along the chromatin axis of the BR gene. Our results suggest that PABPN1 binds to the polymerase before, at, or shortly after the start of transcription, and that the assembly of PABPN1 onto the poly(A) tail may be coupled to transcription. Furthermore, PABPN1 remains associated with the released BR mRNP until the mRNP is translocated from the nucleus to the cytoplasm. (C) 2003 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:332 / 344
页数:13
相关论文
共 54 条
[1]   The human Poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm [J].
Afonina, E ;
Stauber, R ;
Pavlakis, GN .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (21) :13015-13021
[2]   Protein of the SR family of splicing factors binds extensively to exonic Balbiani ring pre-mRNA and accompanies the RNA from the gene to the nuclear pore [J].
AlzhanovaEricsson, AT ;
Sun, X ;
Visa, N ;
Kiseleva, E ;
Wurtz, T ;
Daneholt, B .
GENES & DEVELOPMENT, 1996, 10 (22) :2881-2893
[3]   Transcriptional termination in the Balbiani ring 1 gene is closely coupled to 3′-end formation and excision of the 3′-terminal intron [J].
Baurén, G ;
Belikov, S ;
Wieslander, L .
GENES & DEVELOPMENT, 1998, 12 (17) :2759-2769
[4]  
Becher MW, 2000, ANN NEUROL, V48, P812, DOI 10.1002/1531-8249(200011)48:5<812::AID-ANA20>3.3.CO
[5]  
2-U
[6]   The Drosophila poly(A)-binding protein II is ubiquitous throughout Drosophila development and has the same function in mRNA polyadenylation as its bovine homolog in vitro [J].
Benoit, B ;
Nemeth, A ;
Aulner, N ;
Kühn, W ;
Simonelig, M ;
Wahle, E ;
Bourbon, HM .
NUCLEIC ACIDS RESEARCH, 1999, 27 (19) :3771-3778
[7]   The mRNA assembly line: transcription and processing machines in the same factory [J].
Bentley, D .
CURRENT OPINION IN CELL BIOLOGY, 2002, 14 (03) :336-342
[8]   ASSEMBLY OF A PROCESSIVE MESSENGER-RNA POLYADENYLATION COMPLEX [J].
BIENROTH, S ;
KELLER, W ;
WAHLE, E .
EMBO JOURNAL, 1993, 12 (02) :585-594
[9]   STRUCTURE OF THE CHROMATIN AXIS DURING TRANSCRIPTION [J].
BJORKROTH, B ;
ERICSSON, C ;
LAMB, MM ;
DANEHOLT, B .
CHROMOSOMA, 1988, 96 (05) :333-340
[10]   Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy [J].
Brais, B ;
Bouchard, JP ;
Xie, YG ;
Rochefort, DL ;
Chrétien, N ;
Tomé, FMS ;
Lafrenière, RG ;
Rommens, JM ;
Uyama, E ;
Nohira, O ;
Blumen, S ;
Korcyn, AD ;
Heutink, P ;
Mathieu, J ;
Duranceau, A ;
Codère, F ;
Fardeau, M ;
Rouleau, GA .
NATURE GENETICS, 1998, 18 (02) :164-167