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Titolo:
EVIDENCE THAT THE 60-KDA PROTEIN OF 17S-U2 SMALL NUCLEAR RIBONUCLEOPROTEIN IS IMMUNOLOGICALLY AND FUNCTIONALLY RELATED TO THE YEAST PRP9 SPLICING FACTOR AND IS REQUIRED FOR THE EFFICIENT FORMATION OF PRESPLICEOSOMES
Autore:
BEHRENS SE; GALISSON F; LEGRAIN P; LUHRMANN R;
Indirizzi:
UNIV MARBURG,INST MOLEK BIOL & TUMORFORSCH,EMIL MANNKOPFF STR 2 W-3550 MARBURG GERMANY INST PASTEUR,DEPT BIOL MOLEC F-75724 PARIS 15 FRANCE
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 17, volume: 90, anno: 1993,
pagine: 8229 - 8233
SICI:
0027-8424(1993)90:17<8229:ETT6PO>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRE-MESSENGER-RNA; SPLICEOSOME ASSEMBLY PATHWAY; U2 SNRNP BINDING; SITE SELECTION; U6 SNRNAS; U1; INVITRO; REVEALS; U4/U6; GENES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
S.E. Behrens et al., "EVIDENCE THAT THE 60-KDA PROTEIN OF 17S-U2 SMALL NUCLEAR RIBONUCLEOPROTEIN IS IMMUNOLOGICALLY AND FUNCTIONALLY RELATED TO THE YEAST PRP9 SPLICING FACTOR AND IS REQUIRED FOR THE EFFICIENT FORMATION OF PRESPLICEOSOMES", Proceedings of the National Academy of Sciences of the United Statesof America, 90(17), 1993, pp. 8229-8233

Abstract

Small nuclear ribonucleoprotein (snRNP) U2 functions in the splicing of mRNA by recognizing the branch site of unspliced mRNA. The binding of U2 snRNP and other components to pre-mRNA leads to the formation ofa stable prespliceosome. In HeLa nudear extracts, U2 snRNP exists either as a 17S form (under low salt conditions) or a 12S form (at highersalt concentrations). We have recendy shown that the purified 17S U2 snRNP contains nine proteins with apparent molecular masses of 35, 53,60, 66, 92, 110, 120, 150, and 160 kDa in addition to the common snRNP proteins and the U2 proteins A' and B'' that are found in the 12S U2snRNP form. By using antibodies against the PRP9 protein from Saccharomyces cerevisiae (a protein required for the addition of U2 to prespliceosomes in yeast), we have shown that the 60-kDa protein specific tohuman U2 snRNP particles is structurally related to the yeast PRP9 protein. Interestingly, anti-PRP9 antibodies strongly inhibit prespliceosome formation in HeLa nuckar splking extracts, resulting in a complete inhibition of the mRNA splicing reaction in vitro. This indicates that the U2 60-kDa protein may also be functionally related to its yeastcounterpart PRP9. Most importantly, the addition of purified 17S U2 snRNPs, but not of 12S U2 snRNPs, to HeLa splicing extracts in which the endogeneous U2 snRNPs have been functionally neutralized with anti-PRP9 antibodies fully restores the mRNA-splicing activity of the extracts. These data suggest further that the 17S form is the functionally active form of U2 snRNP in the spliceosome.

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Documento generato il 04/12/20 alle ore 22:32:23