snRNA 3′ end formation requires heterodimeric association of integrator subunits

Molecular and Cellular Biology

Volumn 32, Issue 6, 2012, Pages 1112-1123

  Albrecht, Todd R ^a   Wagner, Eric J ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR; COMPLEMENTARY DNA; HETERODIMER; INTEGRATOR SUBUNIT 11 PROTEIN; INTEGRATOR SUBUNIT 9 PROTEIN; METALLO BETA LACTAMASE; PROTEIN; RNA POLYMERASE II; SMALL NUCLEAR RNA; UNCLASSIFIED DRUG; CARRIER PROTEIN; CPSF3L PROTEIN, HUMAN; INTS9 PROTEIN, HUMAN; RIBONUCLEASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL LYSATE; CELL STRAIN HEK293; CONTROLLED STUDY; CRYSTAL STRUCTURE; DELETION MUTANT; ENZYME ACTIVE SITE; ENZYME BINDING; HELA CELL; HUMAN; IMMUNOPRECIPITATION; IN VITRO STUDY; MOLECULAR CLONING; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN DEPLETION; RNA CLEAVAGE; RNA INTERFERENCE; RNA PROCESSING; RNA TRANSLATION; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; GENE EXPRESSION; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; CARRIER PROTEINS; ENDORIBONUCLEASES; GENE EXPRESSION; HEK293 CELLS; HELA CELLS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; RNA 3' END PROCESSING; RNA, SMALL NUCLEAR;

EID: 84857883120     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.06511-11     Document Type: Article

References (37)

1. Aravind L. 1999. An evolutionary classification of the metallo-betalactamase fold proteins. In Silico Biol. 1:69-91.
2. Baillat D, et al. 2005. Integrator, a multiprotein mediator of small nuclear RNA processing, associates with the C-terminal repeat of RNA polymerase II. Cell 123:265-276.
3. Callebaut I, Moshous D, Mornon JP, de Villartay JP. 2002. Metallobeta-lactamase fold within nucleic acids processing enzymes: the beta- CASP family. Nucleic Acids Res. 30:3592-3601.
4. Chen J, Wagner EJ. 2010. snRNA 3′ end formation: the dawn of the Integrator complex. Biochem. Soc. Trans. 38:1082-1087.
5. Clouet-D'Orval B, Rinaldi D, Quentin Y, Carpousis AJ. 2010. Euryarchaeal beta-CASP proteins with homology to bacterial RNase J have 5′- to 3′-exoribonuclease activity. J. Biol. Chem. 285:17574-17583.
6. Dichtl B, Aasland R, Keller W. 2004. Functions for S. cerevisiae Swd2p in 3′ end formation of specific mRNAs and snoRNAs and global histone 3 lysine 4 methylation. RNA 10:965-977.
7. Dominski Z. 2007. Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism. Crit. Rev. Biochem. Mol. Biol. 42:67-93.
8. Dominski Z, Yang XC, Marzluff WF. 2005. The polyadenylation factor CPSF-73 is involved in histone-pre-mRNA processing. Cell 123:37-48.
9. Dominski Z, Yang XC, Purdy M, Wagner EJ, Marzluff WF. 2005. A CPSF-73 homologue is required for cell cycle progression but not cell growth and interacts with a protein having features of CPSF-100. Mol. Cell. Biol. 25:1489-1500.
10. Egloff S, et al. 2007. Serine-7 of the RNA polymerase II CTD is specifically required for snRNA gene expression. Science 318:1777-1779.
11. Egloff S, O'Reilly D, Murphy S. 2008. Expression of human snRNA genes from beginning to end. Biochem. Soc. Trans. 36:590-594.
12. Egloff S, et al. 2010. The integrator complex recognizes a new double mark on the RNA polymerase II carboxyl-terminal domain. J. Biol. Chem. 285:20564-20569.
13. Ezzeddine N, et al. 2011. A subset of Drosophila integrator proteins is essential for efficient U7 snRNA and spliceosomal snRNA 3′-end formation. Mol. Cell. Biol. 31:328-341.
14. He X, et al. 2003. Functional interactions between the transcription and mRNA3′ end processing machineries mediated by Ssu72 and Sub1. Genes Dev. 17:1030-1042.
15. Hernandez N. 2001. Small nuclear RNA genes: a model system to study fundamental mechanisms of transcription. J. Biol. Chem. 276:26733-26736.
16. Kennedy SA, et al. 2009. Crystal structure of the HEAT domain from the Pre-mRNA processing factor Symplekin. J. Mol. Biol. 392:115-128.
17. Kolev NG, Steitz JA. 2005. Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs. Genes Dev. 19:2583-2592.
18. Kolev NG, Yario TA, Benson E, Steitz JA. 2008. Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′-end maturation. EMBO Rep. 9:1013-1018.
19. Kyburz A, Sadowski M, Dichtl B, Keller W. 2003. The role of the yeast cleavage and polyadenylation factor subunit Ydh1p/Cft2p in pre-mRNA 3′-end formation. Nucleic Acids Res. 31:3936-3945.
20. Li de la Sierra-Gallay I, Zig L, Jamalli A, Putzer H. 2008. Structural insights into the dual activity of RNase J. Nat. Struct. Mol. Biol. 15:206-212.
21. Mandel CR, Bai Y, Tong L. 2008. Protein factors in pre-mRNA 3′-end processing. Cell. Mol. Life Sci. 65:1099-1122.
22. Mandel CR, et al. 2006. Polyadenylation factor CPSF-73 is the pre-mRNA 3′-end-processing endonuclease. Nature 444:953-956.
23. Marzluff WF, Wagner EJ, Duronio RJ. 2008. Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail. Nat. Rev. Genet. 9:843-854.
24. Mathy N, et al. 2007. 5′-to-3′ exoribonuclease activity in bacteria: role of RNase J1 in rRNA maturation and 5′ stability of mRNA. Cell 129:681-692.
25. Mir-Montazeri B, Ammelburg M, Forouzan D, Lupas AN, Hartmann MD. 2011. Crystal structure of a dimeric archaeal cleavage and polyadenylation specificity factor. J. Struct. Biol. 173:191-195.
26. Mount SM, Salz HK. 2000. Pre-messenger RNA processing factors in the Drosophila genome. J. Cell Biol. 150:F37-F44.
27. Murthy KG, Manley JL. 1995. The 160-kD subunit of human cleavagepolyadenylation specificity factor coordinates pre-mRNA 3′-end formation. Genes Dev. 9:2672-2683.
28. Nishida Y, et al. 2010. Crystal structure of an archaeal cleavage and polyadenylation specificity factor subunit from Pyrococcus horikoshii. Proteins 78:2395-2398.
29. Ruepp MD, Schweingruber C, Kleinschmidt N, Schumperli D. 2011. Interactions of CstF-64, CstF-77, and symplekin: implications on localisation and function. Mol. Biol. Cell 22:91-104.
30. Ryan K, Calvo O, Manley JL. 2004. Evidence that polyadenylation factor CPSF-73 is the mRNA 3′ processing endonuclease. RNA 10:565-573.
31. Silva AP, et al. 2011. Structure and activity of a novel archaeal beta-CASP protein with N-terminal KH domains. Structure 19:622-632.
32. Sullivan KD, Steiniger M, Marzluff WF. 2009. A core complex of CPSF73, CPSF100, and Symplekin may form two different cleavage factors for processing of poly(A) and histone mRNAs. Mol. Cell 34:322-332.
33. Takagaki Y, Manley JL. 2000. Complex protein interactions within the human polyadenylation machinery identify a novel component. Mol. Cell. Biol. 20:1515-1525.
34. Wagner EJ, et al. 2007. A genome-wide RNA interference screen reveals that variant histones are necessary for replication-dependent histone prem RNA processing. Mol. Cell 28:692-699.
35. Wagner EJ, et al. 2006. Conserved zinc fingers mediate multiple functions of ZFP100, a U7snRNP associated protein. RNA 12:1206-1218.
36. Xiang K, et al. 2010. Crystal structure of the human symplekin-Ssu72- CTD phosphopeptide complex. Nature 467:729-733.
37. Zhelkovsky A, et al. 2006. The role of the Brr5/Ysh1 C-terminal domain and its homolog Syc1 in mRNA 3′-end processing in Saccharomyces cerevisiae. RNA 12:435-445.