Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′-end maturation

EMBO Reports

Volumn 9, Issue 10, 2008, Pages 1013-1018

  Kolev, Nikolay G ^a   Yario, Therese A ^a   Benson, Eleni ^a   Steitz, Joan A ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR 100; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR 73; ENDONUCLEASE; HISTONE; MESSENGER RNA; METALLO BETA LACTAMASE; PHENANTHROLINE; RIBONUCLEASE; RIBONUCLEASE J; RIBONUCLEASE Z; UNCLASSIFIED DRUG;

3' UNTRANSLATED REGION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; GENETIC CONSERVATION; HUMAN; HUMAN CELL; IN VITRO STUDY; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN MOTIF; RNA PROCESSING;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BASE SEQUENCE; CELL LINE; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR; CONSERVED SEQUENCE; ENDONUCLEASES; ENZYME ACTIVATION; HELA CELLS; HISTONES; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RNA 3' END PROCESSING; RNA PRECURSORS; RNA, MESSENGER;

EUKARYOTA; MAMMALIA;

EID: 53249132654     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2008.146     Document Type: Article

References (21)

1. Aravind L (1999) An evolutionary classification of the metallo-β-lactamase fold proteins. In Silico Biol 1: 69-91
2. Baillat D, Hakimi MA, Näär AM, Shilatifard A, Cooch N, Shiekhattar R (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) Metallo-β-lactamase fold within nucleic acids processing enzymes: The β-CASP family. Nucleic Acids Res 30: 3592-3601
4. de la Sierra-Gallay IL, Zig L, Jamalli A, Putzer H (2008) Structural insights into the dual activity of RNase J. Nat Struct Mol Biol 15: 206-212
5. Dominski Z (2007) Nucleases of the metallo-β-lactamase family and their role in DNA and RNA metabolism. Crit Rev Biochem Mol Biol 42 67-93
6. Dominski Z, Marzluff WF (2007) Formation of the 30 end of histone mRNA: getting closer to the end. Gene 396: 373-390
7. Dominski Z, Yang XC, Marzluff WF (2005a) The polyadenylation factor CPSF-73 is involved in histone-pre-mRNA processing. Cell 123 37-48
8. Dominski Z, Yang XC, Purdy M, Wagner EJ, Marzluff WF (2005b) 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
9. Evans D, Perez I, MacMorris M, Leake D, Wilusz CJ, Blumenthal T (2001) A complex containing CstF-64 and the SL2 snRNP connects mRNA 30 end formation and trans-splicing in C. elegans operons. Genes Dev 15: 2562-2571
10. Gick O, Krämer A, Keller W, Birnstiel ML (1986) Generation of histone mRNA 3′ ends by endonucleolytic cleavage of the pre-mRNA in a snRNP-dependent in vitro reaction. EMBO J 5: 1319-1326
11. Ishikawa H, Nakagawa N, Kuramitsu S, Masui R (2006) Crystal structure of TTHA0252 from Thermus thermophilus HB8, a RNA degradation protein of the metallo-β-lactamase superfamily. J Biochem 140: 535-542
12. Keon BH, Schäfer S, Kuhn C, Grund C, Franke WW(1996) Symplekin, a novel type of tight junction plaque protein. J Cell Biol 134 1003-1018
13. Kolev NG, Steitz JA (2005) Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs. Genes Dev 19: 2583-2592
14. Mandel CR, Kaneko S, Zhang H, Gebauer D, Vethantham V, Manley JL, Tong L (2006) Polyadenylation factor CPSF-73 is the pre-mRNA 3′-end-processing endonuclease. Nature 444: 953-956
15. Mandel CR, Bai Y, Tong L (2008) Protein factors in pre-mRNA 3′-end processing. Cell Mol Life Sci 65: 1099-1122
16. Mathy N, Bénard L, Pellegrini O, Daou R, Wen T, Condon C (2007) 5′-to-3′ exoribonuclease activity in bacteria: Role of RNase J1 in rRNA maturation and 5′ stability of mRNA. Cell 129: 681-692
17. Redko Y, Li de Lasierra-Gallay I, Condon C (2007) When all's zed and done: The structure and function of RNase Z in prokaryotes. Nat Rev Microbiol 5: 278-286
18. Ryan K, Calvo O, Manley JL (2004) Evidence that polyadenylation factor CPSF-73 is the mRNA 3′ processing endonuclease. RNA 10: 565-573
19. Streit A, Koning TW, Soldati D, Melin L, Schümperli D (1993) Variable effects of the conserved RNA hairpin element upon 3′ end processing of histone pre-mRNA in vitro. Nucleic Acids Res 21: 1569-1575
20. Ullu E, Matthews KR, Tschudi C (1993) Temporal order of RNA-processing reactions in trypanosomes: Rapid trans splicing precedes polyadenylation of newly synthesized tubulin transcripts. Mol Cell Biol 13: 720-725
21. Wagner EJ, Burch BD, Godfrey AC, Salzler HR, Duronio RJ, Marzluff WF (2007) A genome-wide RNA interference screen reveals that variant histones are necessary for replication-dependent histone pre-mRNA processing. Mol Cell 28: 692-699