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Titolo:
The nuclear poly(A) binding protein, PABP2, forms an oligomeric particle covering the length of the poly(A) tail
Autore:
Keller, RW; Kuhn, U; Aragon, M; Bornikova, L; Wahle, E; Bear, DG;
Indirizzi:
Univ New Mexico, Hlth Sci Ctr, Dept Cell Biol & Physiol, Albuquerque, NM 87131 USA Univ New Mexico Albuquerque NM USA 87131 ysiol, Albuquerque, NM 87131 USA Univ New Mexico, Hlth Sci Ctr, Ctr Canc, Albuquerque, NM 87131 USA Univ New Mexico Albuquerque NM USA 87131 Canc, Albuquerque, NM 87131 USA Univ Giessen, Inst Biochem, D-35392 Giessen, Germany Univ Giessen Giessen Germany D-35392 t Biochem, D-35392 Giessen, Germany
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 3, volume: 297, anno: 2000,
pagine: 569 - 583
SICI:
0022-2836(20000331)297:3<569:TNPBPP>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRE-MESSENGER-RNA; POLYADENYLATION SPECIFICITY FACTOR; FACTOR I-M; POLY(A)-BINDING PROTEIN; ELECTRON-MICROSCOPY; 3'-END FORMATION; CLEAVAGE; EUKARYOTES; EXPRESSION; POLYMERASE;
Keywords:
polyadenylation; mRNA processing; ribonucleoproteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Bear, DG Univ New Mexico, Hlth Sci Ctr, Dept Cell Biol & Physiol, Albuquerque, NM 87131 USA Univ New Mexico Albuquerque NM USA 87131 buquerque, NM 87131 USA
Citazione:
R.W. Keller et al., "The nuclear poly(A) binding protein, PABP2, forms an oligomeric particle covering the length of the poly(A) tail", J MOL BIOL, 297(3), 2000, pp. 569-583

Abstract

The mammalian nuclear poly(A) binding protein, PABP2, controls the length of the newly synthesized poly(A) tail on messenger RNAs. To gain a better understanding of the mechanism of length control, we have investigated the structure of the PABP2.poly(A) complex. Electron microscopy and scanning force microscopy studies reveal that PABP2, when bound to poly(A), forms both linear filaments and discrete-sized, compact, oligomeric particles. The maximum diameter of the filament is 7 nm; the maximum diameter of the particleis 21(+/-2) nm. Maximum particle size is realized when the PABP2.poly(A) complex is formed with poly(A) molecules 200-300 nt long, which corresponds to the average length of the newly synthesized poly(A) tail in vitro and invivo. The equilibrium between filaments and particles is highly sensitive to ionic strength; filaments are favored at low ionic strength, while particles predominate at moderate to high ionic strength. Nitrocellulose filter binding and gel mobility shift assays indicate that the PABP2.poly(A) particle formed on A(300) is not significantly more stable than complexes formedwith smaller species of poly(A). These results are discussed in the context of the proposed functions for PABP2. (C) 2000 Academic Press.

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Documento generato il 30/11/20 alle ore 06:19:32