How tails define the ending: Divergent roles for polyadenylation in RNA stability and gene expression

RNA Biology

Volumn 7, Issue 1, 2010, Pages

  Glaunsinger, Britt A ^a   Lee, Yeon J ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Herpesvirus; Host shutoff; Hyperadenylation; KSHV; Polyadenylation; RNA export; SOX; TRAMP

Indexed keywords

POLYADENYLATED RNA;

GENE EXPRESSION; HUMAN; NONHUMAN; POLYADENYLATION; POLYMERASE CHAIN REACTION; PROTEIN EXPRESSION; REVIEW; RNA SEQUENCE; RNA STABILITY; RNA TRANSPORT;

EUKARYOTA; HERPESVIRIDAE; HUMAN HERPESVIRUS 8; MAMMALIA; METAZOA;

EID: 85011940617     PISSN: 15476286     EISSN: 15558584     Source Type: Journal    
DOI: 10.4161/rna.7.1.10255     Document Type: Review

References (29)

1. Brodsky AS, Silver PA. Pre-mRNA processing factors are required for nuclear export. RNA 2000; 6:1737-49.
2. Fuke H, Ohno M. Role of poly (A) tail as an identity element for mRNA nuclear export. Nucleic Acids Res 2008; 36:1037-49.
3. Hilleren P, McCarthy T, Rosbash M, Parker R, Jensen TH. Quality control of mRNA 3′-end processing is linked to the nuclear exosome. Nature 2001; 413:538-42.
4. Hilleren P, Parker R. Defects in the mRNA export factors Rat7p, Gle1p, Mex67p and Rat8p cause hyperadenylation during 3′-end formation of nascent transcripts. Rna 2001; 7:753-64.
5. Jensen TH, Patricio K, McCarthy T, Rosbash M. A block to mRNA nuclear export in S. cerevisiae leads to hyperadenylation of transcripts that accumulate at the site of transcription. Mol Cell 2001; 7:887-98.
6. Qu X, Lykke-Andersen S, Nasser T, Saguez C, Bertrand E, Jensen TH, et al. Assembly of an exportcompetent mRNP is needed for efficient release of the 3′-end processing complex after polyadenylation. Mol Cell Biol 2009; 29:5327-38.
7. Ellison KS, Rice SA, Verity R, Smiley JR. Processing of alpha-globin and ICP0 mRNA in cells infected with herpes simplex virus type 1 ICP27 mutants. J Virol 2000; 74:7307-19.
8. Faria PA, Chakraborty P, Levay A, Barber GN, Ezelle HJ, Enninga J, et al. VSV disrupts the Rae1/mrnp41 mRNA nuclear export pathway. Mol Cell 2005; 17:93-102.
9. Saguez C, Schmid M, Olesen JR, Ghazy MA, Qu X, Poulsen MB, et al. Nuclear mRNA surveillance in THO/sub2 mutants is triggered by inefficient polyadenylation. Mol Cell 2008; 31:91-103.
10. Hector RE, Nykamp KR, Dheur S, Anderson JT, Non PJ, Urbinati CR, et al. Dual requirement for yeast hnRNP Nab2p in mRNA poly(A) tail length control and nuclear export. EMBO J 2002; 21:1800-10.
11. Lee Y, Glaunsinger B. Aberrant herpesvirus-induced polyadenylation correlates with cellular messenger RNA destruction. PLoS Biology 2009; 7:1000107.
12. Glaunsinger B, Ganem D. Lytic KSHV infection inhibits host gene expression by accelerating global mRNA turnover. Mol Cell 2004; 13:713-23.
13. Glaunsinger BA, Ganem DE. Messenger RNA turnover and its regulation in herpesviral infection. Adv Virus Res 2006; 66:337-94.
14. Covarrubias S, Richner JM, Clyde K, Lee YJ, Glaunsinger BA. Host Shutoff is a Conserved Phenotype of Gammaherpesvirus Infection and is Orchestrated Exclusively from the Cytoplasm. J Virol 2009.
15. Afonina E, Stauber R, Pavlakis GN. The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm. J Biol Chem 1998; 273:13015-21.
16. Kuhn U, Wahle E. Structure and function of poly(A) binding proteins. Biochim Biophys Acta 2004; 1678:67-84.
17. Brune C, Munchel SE, Fischer N, Podtelejnikov AV, Weis K. Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export. RNA 2005; 11:517-31.
18. Kuehn U, Guendel M, Knoth A, Kerwitz Y, Ruedel S, Wahle E. Poly(A) tail length is controlled by the nuclear poly(A) binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor. J Biol Chem 2009.
19. Rougemaille M, Gudipati RK, Olesen JR, Thomsen R, Seraphin B, Libri D, et al. Dissecting mechanisms of nuclear mRNA surveillance in THO/sub2 complex mutants. EMBO J 2007; 26:2317-26.
20. LaCava J, Houseley J, Saveanu C, Petfalski E, Thompson E, Jacquier A, et al. RNA degradation by the exosome is promoted by a nuclear polyadenylation complex. Cell 2005; 121:713-24.
21. Vanacova S, Wolf J, Martin G, Blank D, Dettwiler S, Friedlein A, et al. A new yeast poly(A) polymerase complex involved in RNA quality control. PLoS Biol 2005; 3:189.
22. Wyers F, Rougemaille M, Badis G, Rousselle JC, Dufour ME, Boulay J, et al. Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase. Cell 2005; 121:725-37.
23. West S, Gromak N, Norbury CJ, Proudfoot NJ. Adenylation and exosome-mediated degradation of cotranscriptionally cleaved pre-messenger RNA in human cells. Mol Cell 2006; 21:437-43.
24. Glaunsinger B, Chavez L, Ganem D. The exonuclease and host shutoff functions of the SOX protein of Kaposi's sarcoma-associated herpesvirus are genetically separable. J Virol 2005; 79:7396-401.
25. Couttet P, Fromont-Racine M, Steel D, Pictet R, Grange T. Messenger RNA deadenylylation precedes decapping in mammalian cells. Proc Natl Acad Sci USA 1997; 94:5628-33.
26. Mullen TE, Marzluff WF. Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5′ to 3′ and 3′ to 5′. Genes Dev 2008; 22:50-65.
27. Radford HE, Meijer HA, de Moor CH. Translational control by cytoplasmic polyadenylation in Xenopus oocytes. Biochim Biophys Acta 2008; 1779:217-29.
28. Schuster G, Stern D. RNA polyadenylation and decay in mitochondria and chloroplasts. Prog Mol Biol Transl Sci 2009; 85:393-422.
29. Slomovic S, Laufer D, Geiger D, Schuster G. Polyadenylation and degradation of human mitochondrial RNA: the prokaryotic past leaves its mark. Mol Cell Biol 2005; 25:6427-35.