The polyadenylation factor CstF-64 regulates alternative processing of IgM heavy chain pre-mRNA during B cell differentiation

Cell

Volumn 87, Issue 5, 1996, Pages 941-952

  Takagaki, Yoshio ^a   Seipelt, Rebecca L ^b   Peterson, Martha L ^b   Manley, James L ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b UNIVERSITY OF KENTUCKY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN MU CHAIN; MESSENGER RNA;

ANIMAL CELL; ARTICLE; B LYMPHOCYTE DIFFERENTIATION; GROWTH REGULATION; IMMUNOGLOBULIN PRODUCTION; MOUSE; NONHUMAN; POLYADENYLATION; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN SYNTHESIS REGULATION;

ANIMALIA; MUS;

EID: 0030606286     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)82000-0     Document Type: Article

References (48)

1. Alt, F.W., Bothwell, A.L.M., Knapp, M., Siden, E., Mather, E., Koshland, M., and Baltimore, D. (1980). Synthesis of secreted and membrane-bound immunoglobulin μ heavy chains is directed by mRNAs that differ at their 3′ ends. Cell 20, 293-301.
2. Beyer, A.L., and Osheim, Y.N. (1988). Splice site selection, rate of splicing, and alternative splicing on nascent transcripts. Genes Dev. 2, 754-765.
3. Blattner, F.R., and Tucker, P.W. (1984). The molecular biology of immunoglobulin D. Nature 307, 417-422.
4. Buerstedde, J.-M., Reynaud, C.-A., Humphries, E.H., Olson, W., Ewert, D.L., and Weill, J.-C. (1990). Light chain gene conversion continues at high rate in an ALV-induced cell line. EMBO J. 9, 921-927.
5. Buerstedde, J.-M., and Takeda, S. (1991). Increased ratio of targeted to random integration after transfection of chicken B cell lines. Cell 67, 179-188.
6. Cáceres, J.F., Stamm, S., Helfman, D.M., and Krainer, A.R. (1994). Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors. Science 265, 1706-1709.
7. Ceredig, R., Lowenthal, J.W., Nabholz, M., and MacDonald, H.R. (1985). Expression of interleukin-2 receptors as a differentiation marker on intrathymic stem cells. Nature 314, 98-100.
8. Chomczynski, P., and Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
9. DeBenedette, M., and Snow, E.C. (1991). Induction and regulation of casein kinase II during B lymphocyte activation. J. Immunol. 147, 2839-2845.
10. Early, P., Rogers, J., Davis, M., Calame, K., Bond, M., Wall, R., and Hood, L. (1980). Two mRNAs can be produced from a single immunoglobulin μ gene by alternative RNA processing pathways. Cell 20, 313-319.
11. Edwalds-Gilbert, G., and Milcarek, C. (1995). Regulation of poly(A) site use during mouse B-cell development involves a change in the binding of a general polyadenylation factor in a B-cell stage-specific manner. Mol. Cell. Biol. 15, 6420-6429.
12. Field, J., Nikawa, J.-I., Broek, D., MacDonald, B., Rodgers, L., Wilson, I.A., Lerner, R.A., and Wigler, M. (1988). Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method. Mol. Cell. Biol. 8, 2159-2165.
13. Foulkes, N.S., Schlotter, F., Pevet, P., and Sassone-Corsi, P. (1993). Pituitary hormone FSH directs the CREM functional switch during spermatogenesis. Nature 362, 264-267.
14. Ge, H., and Manley, J.L. (1990). A protein factor, ASF, controls cell-specific alternative splicing of SV40 early pre-mRNA in vitro. Cell 62, 25-34.
15. Gilmartin, G.M., and Nevins, J.R. (1991). Molecular analyses of two poly(A) site-processing factors that determine the recognition and efficiency of cleavage of the pre-mRNA. Mol. Cell. Biol. 11, 2432-2438.
16. Guise, J.W., Lim, P.L., Yuan, D., and Tucker, P.W. (1988). Alternative expression of secreted and membrane forms of immunoglobulin μ-chain is regulated by transcriptional termination in stable plasmacytoma transfectants. J. Immunol. 140, 3988-3994.
17. Guise, J.W., Galli, G., Nevins, J.R., and Tucker, P.W. (1989). Developmental regulation of secreted and membrane forms of immunoglobulin μ chain. In Immunoglobulin Genes, T. Honjo, F.W. Alt, and T.H. Rabbitts, eds. (London: Academic Press), pp. 275-301.
18. Harlow, E., and Lane, D. (1988). Antibodies: A Laboratory Manual (Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press).
19. Jenny, A., Hauri, H.-P., and Keller, W. (1994). Characterization of cleavage and polyadenylation specificity factor and cloning of its 100-kilodalton subunit. Mol. Cell. Biol. 14, 8183-8190.
20. Keller, W. (1995). No end yet to messenger RNA 3′ processing! Cell 81, 829-832.
21. Krainer, A.R., Conway, G.C., and Kozak, D. (1990). The essential pre-mRNA splicing factor SF2 influences 5′ splice site selection by activating proximal sites. Cell 62, 35-42.
22. MacDonald, C.C., Wilusz, J., and Shenk, T. (1994). The 64-kilodalton subunit of the CstF polyadenylation factor binds to pre-mRNAs downstream of the cleavage site and influences cleavage site location. Mol. Cell. Biol. 14, 6647-6654.
23. Mandart, E., and Parker, R. (1995). Effects of mutations in the Saccharomyces cerevisiae RNA14, RNA15, and PAP1 genes on polyadenylation in vivo. Mol. Cell Biol. 15, 6979-6986.
24. Manley, J.L. (1995). A complex protein assembly catalyzes polyadenylation of mRNA precursors. Curr. Opin. Genet. Dev. 5, 222-228.
25. Manley, J.L., Sharp, P.A., and Gefter, M.L. (1982). RNA synthesis in isolated nuclei: processing of adenovirus serotype 2 late messenger RNA precursors. J. Mol. Biol. 159, 581-599.
26. Mann, K.P., Weiss, E.A., and Nevins, J.R. (1993). Alternative poly(A) site utilization during adenovirus infection coincides with a decrease in the activity of a poly(A) site processing factor. Mol. Cell. Biol. 13, 2411-2419.
27. Minvielle-Sebastia, L., Winsor, B., Bonneaud, N., and Lacroute, F. (1991). Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA decay rate; sequence analysis reveals an RNA-binding domain in the RNA15 protein. Mol. Cell. Biol. 11, 3075-3087.
28. Minvielle-Sebastia, L., Preker, P.J., and Keller, W. (1994). RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3′-end processing factor. Science 266, 1702-1705.
29. Mitchelson, A., Simonelig, M., Williams, C., and O'Hare, K. (1993). Homology with S. cerevisiae RNA 14 suggests that phenotypic suppression in Drosophila by suppressor of forked occurs at the level of RNA stability. Genes Dev. 7, 241-249.
30. Murthy, K.G.K., and Manley, J.L. (1992). Characterization of the multisubunit cleavage-polyadenylation specificity factor from calf thymus. J. Biol. Chem. 267, 14804-14811.
31. Murthy, K.G.K., and Manley, J.L. (1995). The 160-kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3′-end formation. Genes Dev. 9, 2672-2683.
32. + nuclear sequences are conserved and poly(A) addition precedes splicing. Cell 15, 1477-1493.
33. O'Hare, K. (1995). mRNA 3′ ends in focus. Trends Genet. 11, 255-257.
34. Peterson, M.L. (1994a). RNA processing and expression of immunoglobulin genes. In Handbook of B and T Lymphocytes, E.C. Snow, ed. (San Diego, California: Academic Press), pp. 321-342.
35. Peterson, M.L. (1994b). Regulated immunoglobulin (Ig) RNA processing does not require specific cis-acting sequences: non-Ig RNA can be alternatively processed in B cells and plasma cells. Mol. Cell. Biol. 14, 7891-7898.
36. Peterson, M.L., and Perry, R.P. (1986). Regulated production of μm and μs mRNA requires linkage of the poly(A) addition sites and is dependent on the length of the μs-μm intron. Proc. Natl. Acad. Sci. USA 83, 8883-8887.
37. Peterson, M.L., Gimmi, E.R., and Perry, R.P. (1991). The developmentally regulated shift from membrane to secreted μ mRNA production is accompanied by an increase in cleavage-polyadenylation efficiency but no measurable change in splicing efficiency. Mol. Cell. Biol. 11, 2324-2327.
38. Proudfoot, N. (1991). Poly(A) signals. Cell 64, 671-674.
39. Rogers, J., Early, P., Carter, C., Calame, K., Bond, M., Hood, L., and Wall, R. (1980). Two mRNAs with different 3′ ends encode membrane-bound and secreted forms of immunoglobulin μ chain. Cell 20, 303-312.
40. Roth, M.B., Murphy, C., and Gall, J.G. (1990). A monoclonal antibody that recognizes a phosphorylated epitope stains lampbrush chromosome loops and small granules in the amphibian germinal vesicle. J. Cell Biol. 111, 2217-2223.
41. Takagaki, Y., Ryner, L.C., and Manley, J.L. (1989). Four factors are required for 3′-end cleavage of pre-mRNAs. Genes Dev. 3, 1711-1724.
42. Takagaki, Y., Manley, J.L., MacDonald, C.C., Wilusz, J., and Shenk, T. (1990). A multisubunit factor, CstF, is required for polyadenylation of mammalian pre-mRNAs. Genes Dev. 4, 2112-2120.
43. Takagaki, Y., MacDonald, C.C., Shenk, T., and Manley, J.L. (1992). The human 64-kDa polyadenylation factor contains a ribonucleo-protein-type RNA binding domain and unusual auxiliary motifs. Proc. Natl. Acad. Sci. USA 89, 1403-1407.
44. Takagaki, Y., and Manley, J.L. (1992). A human polyadenylation factor is a G protein β-subunit homologue. J. Biol. Chem. 267, 23471-23474.
45. Takagaki, Y., and Manley, J.L. (1994). A polyadenylation factor subunit is the human homologue of the Drosophila suppressor of forked protein. Nature 372, 471-474.
46. Wang, J., and Manley, J.L. (1995). Overexpression of the SR proteins ASF/SF2 and SC35 influences alternative splicing in vivo in diverse ways. RNA 1, 335-346.
47. Yan, D.-H., Weiss, E.A., and Nevins, J.R. (1995). Identification of an activity in B-cell extracts that selectively impairs the formation of an immunoglobulin μs poly(A) site processing complex. Mol. Cell. Biol. 15, 1901-1906.
48. Zahler, A.M., Neugebauer, K.M., Lane, W.S., and Roth, M.B. (1993). Distinct functions of SR proteins in alternative pre-mRNA splicing. Science 260, 219-222.