SLBP is associated with histone mRNA on polyribosomes as a component of the histone mRNP

Nucleic Acids Research

Volumn 32, Issue 16, 2004, Pages 4833-4842

  Whitfield, Michael L ^a,b,c   Kaygun, Handan ^b   Erkmann, Judith A ^a,b   Townley Tilson, W H Davin ^c   Dominski, Zbigniew ^a,b   Marzluff, William F ^a,b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

^c DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CYCLOHEXIMIDE; HISTONE; MESSENGER RNA; RIBONUCLEOPROTEIN; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR; DNA; MESSENGER RIBONUCLEOPROTEIN; NUCLEAR PROTEIN; NUCLEIC ACID SYNTHESIS INHIBITOR; RNA PRECURSOR; SLBP PROTEIN, HUMAN; SLBP PROTEIN, MOUSE;

3' UNTRANSLATED REGION; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOPLASM; DNA REPLICATION; IMMUNOPRECIPITATION; INTRACELLULAR TRANSPORT; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYSOME; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN SYNTHESIS; PROTEIN TRANSPORT; RNA BINDING; ANIMAL; BIOSYNTHESIS; CELL CULTURE; CELL NUCLEUS; CHEMISTRY; CHO CELL; CRICETULUS; DRUG EFFECT; GENETICS; HAMSTER; HUMAN; IMMUNOLOGY; METABOLISM; SERODIAGNOSIS;

ANIMALS; CELL NUCLEUS; CHO CELLS; CRICETINAE; CRICETULUS; CYCLOHEXIMIDE; DNA; DNA REPLICATION; HISTONES; HUMANS; MICE; MRNA CLEAVAGE AND POLYADENYLATION FACTORS; NUCLEAR PROTEINS; NUCLEIC ACID SYNTHESIS INHIBITORS; POLYRIBOSOMES; PRECIPITIN TESTS; RIBONUCLEOPROTEINS; RNA PRECURSORS; RNA, MESSENGER; TUMOR CELLS, CULTURED;

EID: 4444235108     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh798     Document Type: Article

References (62)

1. Marzluff,W.F. (1992) Histone 3′ ends: essential and regulatory functions. Gene Expr., 2, 93-97.
2. Dominski,Z. and Marzluff,W.F. (1999) Formation of the 3′ end of histone mRNA. Gene, 239, 1-14.
3. Gallie,D.R. (1998) A tale of two termini: a functional interaction between the termini of an mRNA is a prerequisite for efficient translation initiation. Gene, 216, 1-11.
4. Sachs,A.B., Sarnow,P. and Hentze,M.W. (1997) Starting at the beginning, middle, and end: translation initiation in eukaryotes. Cell 89, 831-838.
5. Jacobson,A. (1996) PolyA metabolism and translation: the closed loop model. In Hershey,J.W., Mathews,M.B. and Sonenberg,N. (eds), Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 451-480.
6. Sun,J.-H., Pilch,D.R. and Marzluff,W.F. (1992) The histone mRNA 3′ end is required for localization of histone mRNA to polyribosomes. Nucleic Acids Res., 20, 6057-6066.
7. Gallie,D.R., Lewis,N.J. and Marzluff,W.F. (1996) The histone 3′-terminal stem-loop is necessary for translation in Chinese hamster ovary cells. Nucleic Acids Res., 24, 1954-1962.
8. Sanchez,R. and Marzluff,W.F. (2002) The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro. Mol. Cell. Biol., 22, 7093-7104.
9. Harris,M.E., Böhni,R., Schneiderman,M.H., Ramamurthy,L., Schümperli,D. and Marzluff,W.F. (1991) Regulation of histone, mRNA in the unperturbed cell cycle: Evidence suggesting control at two posttranscriptional steps. Mol. Cell. Biol., 11, 2416-2424.
10. Sariban,E., Wu,R.S., Erickson,L.C. and Bonner,W.M. (1985) Interrelationships of protein and DNA syntheses during replication of mammalian cells. Mol. Cell. Biol., 5, 1279-1286.
11. Sittman,D.B., Graves,R.A. and Marzluff,W.F. (1983) Historic mRNA concentrations are regulated at the level of transcription and mRNA degradation. Proc. Natl Acad. Sci. USA, 80, 1849-1853.
12. Graves,R.A. and Marzluff,W.F. (1984) Rapid, reversible alterations in histone gene transcription and histone mRNA levels in mouse myeloma cells. Mol. Cell. Biol., 4, 351-357.
13. Pandey,N.B. and Marzluff,W.F. (1987) The stem-loop structure at the 3′ end of histone mRNA is necessary and sufficient for regulation of histone mRNA stability. Mol. Cell. Biol., 7, 4557-4559.
14. Ross,J., Peltz,S.W., Kobs,G. and Brewer,G. (1986) Histone mRNA degradation in vivo: the first detectable step occurs at or near the 3′ terminus. Mol. Cell. Biol., 6, 4362-4371.
15. Ross,J., Kobs,G., Brewer,G. and Peltz,S.W. (1987) Properties of the exonuclease activity that degrades H4 histone mRNA. J. Biol. Chem., 262, 9374-9381.
16. Caruccio,N. and Ross,J. (1994) Purification of a human polyribosome-associated 3′ to 5′ exonuclease. J. Biol. Chem., 269, 31814-31821.
17. Dominski,Z., Yang,X., Kaygun,H. and Marzluff,W.F. (2003) A 3′ exonuclease that specifically interacts with the 3′ end of histone mRNA. Mol. Cell, 12, 295-305.
18. Wang,Z.-F., Whitfield,M.L., Ingledue,T.I., Dominski,Z. and Marzluff,W.F. (1996) The protein which binds the 3′ end of histone mRNA: a novel RNA- binding protein required for histone pre-mRNA processing. Genes Dev., 10, 3028-3040.
19. Martin,F., Schaller,A., Eglite,S., Schümperli,D. and Müller,B. (1997) The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein. EMBO J., 16, 769-778.
20. Dominski,Z., Zheng,L.-X., Sanchez,R. and Marzluff,W.F. (1999) The stem-loop binding protein facilitates 3′ end formation by stabilizing U7 snRNP binding to the histone pre-mRNA. Mol. Cell. Biol. 19, 3561-3570.
21. Marzluff,W.F. and Duronio,R.J. (2002) Histone mRNA expression: multiple levels of cell cycle regulation and important developmental consequences. Curr. Opin. Cell Biol., 14, 692-699.
22. Whitfield,M.L., Zheng,L.-X., Baldwin,A., Ohta,T., Hurt,M.M. and Marzluff,W.F. (2000) Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms. Mol. Cell. Biol., 20, 4188-4198.
23. Zheng,L.-X., Dominski,Z., Yang,X., Elms,P., Raska,C.S., Borchers,C.H. and Marzluff,W.F. (2003) Phosphorylation of SLBP on two threonines triggers degradation of SLBP, the sole cell-cycle regulated factor required for regulation of histone mRNA processing, at the end of S-phase. Mol. Cell. Biol., 23, 1590-1601.
24. Hanson,R.J., Sun,J.-H., Willis,D.G. and Marzluff,W.F. (1996) Efficient extraction and partial purification of the polyribosomal-associated stem-loop binding protein bound to the 3′ end of histone mRNA. Biochemistry, 35, 2146-2156.
25. Marzluff,W.F., Whitfield,M.L., Dominski,Z. and Wang,Z.-F. (1997) Identification of the protein that interacts with the 3′ end of histone mRNA. In Richter,J.D. (ed.), mRNA Formation and Function. Academic Press, NY, pp. 163-193.
26. Graves,R.A., Wellman,S.E., Chiu,I.-M. and Marzluff,W.F. (1985) Differential expression of two clusters of mouse histone genes. J. Mol. Biol., 183, 179-194.
27. Wang,Z.-F., Sirotkin,A.M., Buchold,G.M., Skoultchi,A.I. and Marzluff,W.F. (1997) The mouse histone H1 genes: gene organization and differential regulation. J. Mol. Biol., 271, 124-138.
28. Pandey,N.B., Sun,J.-H. and Marzluff,W.F. (1991) Different complexes are formed on the 3′ end of histone mRNA in nuclear and polysomal extracts. Nucleic Acids Res., 19, 5653-5659.
29. Schochetman,G. and Perry,R.P. (1972) Early appearance of histone messenger RNA in polyribosomes of cultured L cells. J. Mol. Biol., 63, 591-596.
30. Michel,J.J. and Xiong,Y. (1998) Human CUL-1, but not other cullin family members, selectively interacts with SKP1 to form a complex with SKP2 and cyclin A. Cell Growth Differ., 9, 435-449.
31. Wells,D. and Kedes,L. (1985) Structure of a human histone cDNA: evidence that basally expressed histone genes have intervening sequences and encode polyadenylated mRNAs. Proc. Natl Acad. Sci. USA 82, 2834-2838.
32. Marzluff,W.F., Gongidi,P., Woods,K.R., Jin,J.P. and Maltais,L. (2002) The human and mouse replication-dependent histone genes. Genomics, 80, 487-498.
33. Pilch,D.R. and Marzluff,W.F. (1991) Expression of histone-U1 snRNA genes: U1 promoters are compatible with historic 3′ end formation. Gene Expr., 1, 41-53.
34. Stimac,E., Groppi,V.E.,Jr and Coffino,P. (1984) Inhibition of protein synthesis stabilizes histone mRNA. Mol. Cell. Biol., 4 2082-2087.
35. Baumbach,L.L., Marashi,F., Plumb,M., Stein,G. and Stein,J. (1984) Inhibition of DNA replication coordinately reduces cellular levels of core and H1 histone mRNAs: requirement for protein synthesis. Biochemistry, 23, 1618-1625.
36. Lüscher,B., Stauber,C., Schindler,R. and Schümperli,D. (1985) Faithful cell-cycle regulation of a recombinant mouse histone H4 gene is controlled by sequences in the 3′-terminal part of the gene. Proc. Natl Acad. Sci. USA, 82, 4389-4393.
37. Stauber,C., Lüscher,B., Eckner,R., Lotscher,E. and Schümperli,D. (1986) A signal regulating mouse histone H4 mRNA levels in a mammalian cell cycle mutant and sequences controlling RNA 3′ processing are both contained within the same 80-bp fragment. EMBO J. 5, 3297-3303.
38. Stauber,C. and Schümperli,D. (1988) 3′ processing of pre-mRNA plays a major role in proliferation-dependent regulation of histone gene expression. Nucleic Acids Res., 16, 9399-9413.
39. Butler,W.B. and Mueller,G.C. (1973) Control of histone synthesis in HeLa cells. Biochim. Biophys. Acta, 294, 481-496.
40. Williams,A.S. and Marzluff,W.F. (1995) The sequence of the stem and flanking sequences at the 3′ end of histone mRNA are critical determinants for the binding of the stem-loop binding protein. Nucleic Acids Res., 23, 654-662.
41. Ishigaki,Y., Li,X.J., Serin,G. and Maquat,L.E. (2001) Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20. Cell, 106, 607-617.
42. Wahle,E. (1991) A novel poly(A)-binding protein acts as a specificity factor in the second phase of messenger RNA polyadenylation. Cell, 66, 759-768.
43. Imataka,H., Gradi,A. and Sonenberg,N. (1998) A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J., 17, 7480-7489.
44. Kessler,S.H. and Sachs,A.B. (1998) RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G. Mol. Cell. Biol., 18, 51-57.
45. Chkheidze,A.N., Lyakhov,D.L., Makeyev,A.V., Morales,J., Kong,J. and Liebhaber,S.A. (1999) Assembly of the α-globin mRNA stability complex reflects binary interaction between the pyrimidine-rich 3′ untranslated region determinant and poly(C) binding protein αCP. Mol. Cell. Biol., 19, 4572-4581.
46. Kiledjian,M., Wang,X.M. and Liebhaber,S.A. (1995) Identification of two KH domain proteins in the α-globin mRNP stability complex. EMBO J., 14, 4357-4364.
47. 2 and the 3′-untranslated region of collagen α1(I) mRNA. Nucleic Acids Res., 28, 4306-4316.
48. Antic,D., Lu,N. and Keene,J.D. (1999) ELAV tumor antigen, Hel-N1, increases translation of neurofilament M mRNA and induces formation of neurites in human teratocarcinoma cells. Genes Der., 13, 449-461.
49. Jain,R.G., Andrews,L.G., McGowan,K.M., Pekala,P.H. and keene,J.D. (1997) Ectopic expression of Hel-N1, an RNA-binding protein, increases glucose transporter (GLUT1) expression in 3T3-L1 adipocytes. Mol. Cell. Biol., 17, 954-962.
50. Fan,X.H. and Steitz,J.A. (1998) Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs. EMBO J., 17, 3448-3460.
51. Peng,S.S., Chen,C.Y., Xu,N.H. and Shyu,A.B. (1998) RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein. EMBO J., 17, 3461-3470.
52. Loflin,P., Chen,C.Y.A. and Shyu,A.B. (1999) Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element. Genes Der., 13, 1884-1897.
53. DeMaria,C.T. and Brewer,G. (1996) AUF1 binding affinity to A + U-rich elements correlates with rapid mRNA degradation. J. Biol. Chem., 271, 12179-12184.
54. D'Agostino,D.M., Felber,B.K., Harrison,J.E. and Pavlakis,G.N. (1992) The Rev protein of human immunodeficiency virus type 1 promotes polysomal association and translation of gag/pol and vpu /env mRNAs. Mol. Cell. Biol., 12, 1375-1386.
55. Kalland,K.-H., Szilvay,A.M., Brokstad,K.A., Sætrevik,W. and Haukenes,G. (1994) The human immunodeficiency virus type 1 Rev protein shuttles between the cytoplasm and nuclear compartments. Mol. Cell. Biol., 14, 7436-7444.
56. Le Hir,H., Moore,M.J. and Maquat,L.E. (2000) Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions. Genes Dev., 14, 1098-1108.
57. Le Hir,H., Izaurralde,E., Maquat,L.E. and Moore,M.J. (2000) The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J., 19, 6860-6869.
58. Grosset,C., Chen,C.Y.A., Xu,N.H., Sonenberg,N., Jacquemin-Sablon,H. and Shyu,A.B. (2000) A mechanism for translationally coupled mRNA turnover: Interaction between the poly(A) tail and a c- fos RNA coding determinant via a protein complex. Cell, 103 29-40.
59. Shyu,A.B. and Wilkinson,M.F. (2000) The double lives of shuttling mRNA binding proteins. Cell, 102, 135-138.
60. Bernstein,P. and Ross,J. (1989) Poly(A), poly(A) binding protein and the regulation of mRNA stability. Trends Biochem. Sci., 14, 373-377.
61. Ross,J. and Kobs,G. (1986) H4 histone messenger RNA decay in cell-free extracts initiates at or near the 3′ terminus and proceeds 3′ to 5′. J. Mol. Biol., 188, 579-593.
62. Whitfield,M.L., SherlockG., Saldanha,A.J., Murray,J.I., Ball,C.A., Alexander,K.E., Matese,J.C., Perou,C.M., Hurt,M.M., Brown,P.O. et al. (2002) Identification of genes periodically expressed in the human cell cycle and their expression in tumors. Mol. Biol. Cell, 13, 1977-2000.