Inhibition of msl-2 splicing by Sex-lethal reveals interaction between U2AF35 and the 3' splice site AG

Nature

Volumn 402, Issue 6763, 1999, Pages 838-841

  Merendino, Livia ^a   Guth, Sabine ^a   Bilbao, Daniel ^a   Martínez, Concepción ^a   Valcárcel, Juan ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; DINUCLEOTIDE; PYRIMIDINE DERIVATIVE; SPLICING FACTOR U2AF; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; DROSOPHILA; GENE DOSAGE; HUMAN; HUMAN CELL; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INTERACTION; RNA SPLICING; SPECIES DIFFERENCE; SPLICEOSOME;

ADENINE NUCLEOTIDES; BINDING SITES; DNA-BINDING PROTEINS; DROSOPHILA PROTEINS; GUANINE NUCLEOTIDES; HELA CELLS; HUMANS; INTRONS; NUCLEAR PROTEINS; PROTEIN BINDING; RIBONUCLEOPROTEINS; RNA PRECURSORS; RNA SPLICING; RNA-BINDING PROTEINS; TRANSCRIPTION FACTORS;

EID: 0033576625     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/45602     Document Type: Article

References (22)

1. Bashaw, G. & Baker, B. The msl-2 dosage compensation gene of Drosophila encodes a putative DNA-binding protein whose expression is sex specifically regulated by Sex-lethal. Development 121, 3245-3258 (1995).
2. Kelley, R. et al. Expression of Msl-2 causes assembly of dosage compensation regulators on the X chromosomes and female lethality in Drosophila. Cell 81, 867-877 (1995).
3. Zhou, S. et al. Male-specific lethal 2, a dosage compensation gene of Drosophila, undergoes sex-specific regulation and encodes a protein with RING finger and a metallothionein-like cystein cluster. EMBO J. 14, 2884-2895 (1995).
4. Bashaw, G. & Baker, B. The regulation of the Drosophila msl-2 gene reveals a function for Sex-lethal in translational control. Cell 89, 789-798 (1997).
5. Kelley, R., Wang, J., Bell, L. & Kuroda, M. Sex-lethal controls dosage compensation in Drosophila by a non-splicing mechanism. Nature 387, 195-199 (1997).
6. Gebauer, F., Merendino, L., Hentze, M. & Valcárcel, J. The Drosophila splicing regulator Sex-lethal directly inhibits translation of male-specific-lethal 2 mRNA. RNA 4, 142-150 (1998).
7. Zamore, P. & Green, M. Identification, purification and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor. Proc. Natl Acad. Sci. USA 86, 9243-9247 (1989).
8. Zamore, P., Patton, J. & Green, M. R. Cloning and domain structure of the mammalian splicing factor U2AF. Nature 335, 609-614 (1992).
9. Zuo, P. & Maniatis, T. The splicing factor U2AF35 mediates critical protein-protein interactions in constitutive and enhancer-dependent splicing. Genes Dev. 10, 1356-1368 (1996).
10. Kan, J. & Green, M. R. Pre-mRNA splicing of IgM exons M1 and M2 is directed by juxtaposed splicing enhancer and inhibitor. Genes Dev. 13, 462-471 (1999).
11. Singh, R., Valcárcel, J. & Green, M. Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins. Science 268, 1173-1176 (1995).
12. Zamore, P. D. & Green, M. R. Biochemical characterization of U2 snRNP auxiliary factor: an essential pre-mRNA splicing factor with a novel intranuclear distribution. EMBO J. 10, 207-214 (1991).
13. Valcárcel, J., Singh, R., Zamore, P. & Green, M. R. The protein Sex-lethal antagonizes the splicing factor U2AF to regulate alternative splicing of transformer pre-mRNA. Nature 362, 171-175 (1993).
14. Frank, D. & Guthrie, C. An essential splicing factor, SLU7, mediates 3′ splice site choice in yeast. Genes Dev. 6, 2112-2124 (1992).
15. Umen, J. G. & Guthrie, C. The second catalytic step of pre-mRNA splicing. RNA 1, 869-885 (1995).
16. Luukkonen, B. G. M. & Seraphin, B. The roles of branchpoint-3′ splice site spacing and interaction between intron-terminal nucleotides in 3′ splice site selection in Saccharomyces cerevisiae. EMBO J. 16, 779-792 (1997).
17. Reed, R. The organization of 3′ splice-site sequences in mammalian introns. Genes Dev. 3, 2113-2123 (1989).
18. Smith, C. W. J., Chu, T. T. & Nadal-Ginard, B. Scanning and competition between AGs are involved in 3′ splice site selection in mammalian introns. Mol. Cell. Biol. 13, 4939-4952 (1993).
19. Chiara, M. D., Palandjian, I., Feld Kramer, R. & Reed, R. Evidence that U5 snRNP recognizes the 5′ splice site for catalytic step II in mammals. EMBO J. 16, 4746-4759 (1997).
20. Zapp, M. L. & Betget, S. M. Evidence for nuclear factors involved in recognition of 5′ splice sites. Nucleic Acids Res. 17, 2655-2674 (1989).
21. Dignam, J., Lebovitz, R. & Roeder, R. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11, 1475-1489 (1983).
22. Moore, M. & Sharp, P. Site-specific modification of pre-mRNA: the 2′ hydroxyl groups at the splice sites. Science 256, 992-997 (1992).