The half-life of RAG-1 protein in precursor B cells is increased in the absence of RAG-2 expression

Journal of Experimental Medicine

Volumn 183, Issue 4, 1996, Pages 1731-1737

  Grawunder, Ulf ^a,c   Schatz, David G ^b   Leu, Thomas M J ^b   Rolink, Antonius ^a   Melchers, Fritz ^a  

^a BASEL INSTITUTE FOR IMMUNOLOGY   (Switzerland)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN; INTERLEUKIN 7; MESSENGER RNA; T LYMPHOCYTE RECEPTOR;

ANIMAL CELL; ARTICLE; B LYMPHOCYTE DIFFERENTIATION; BONE MARROW CELL; FETUS; GENE EXPRESSION; GENETIC RECOMBINATION; HALF LIFE TIME; LIVER CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN METABOLISM; PROTEIN PROCESSING; PROTEIN SYNTHESIS; RECEPTOR GENE; TRANSGENIC MOUSE;

ANIMALS; B-LYMPHOCYTES; DNA-BINDING PROTEINS; FEMALE; GENE EXPRESSION REGULATION; HALF-LIFE; HEMATOPOIETIC STEM CELLS; HOMEODOMAIN PROTEINS; MALE; MICE; MICE, INBRED STRAINS; MICE, MUTANT STRAINS; MICE, TRANSGENIC; PROTEIN BIOSYNTHESIS; PROTEINS; RECOMBINATION, GENETIC; RNA, MESSENGER;

EID: 0029978830     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.183.4.1731     Document Type: Article

References (36)

1. Tonegawa, S. 1983. Somatic generation of antibody diversity. Nature (Lond.). 302:575-581.
2. Schatz, D.G., M.A. Oettinger, and D. Baltimore. 1989. The V(D)J recombination activating gene, RAG-1. Cell. 59: 1035-1048.
3. Oettinger, M.A., D.G. Schatz, C. Gorka, and D. Baltimore. 1990. RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination Science (Wash. DC). 248:1517-1523.
4. Schatz, D.G., and D. Baltimore. 1988. Stable expression of immunoglobulin gene V(D)J recombinase activity by gene transfer into 3T3 fibroblasts. Cell. 53:107-115.
5. Shinkai, Y., G. Rathbun, K.P. Lam, E.M. Oltz, V. Stewart, M. Mendelsohn, J. Charron, M. Datta, R. Young, A.M. Stall, and F.W. Alt. 1992. RAG-2-deficient mice lack mature lymphocytes owing to inability to initiate V(D)J rearrangement. Cell. 68:855-867.
6. Mombaerts, P., J. Iacomim, R.S. Johnson, K. Herrup, S. Tonegawa, and V E. Papaioannou. 1992. RAG-1-deficient mice have no mature B and T lymphocytes. Cell. 68:869-877.
7. Blunt, T., N.J. Finnie, G.E. Taccioli, G.C.M. Smith, J. Demengeot, T.M. Gottlieb, R. Mizuta, A.J. Varghese, F.W. Alt, P.A. Jeggo, and S.P. Jackson. 1995. Defective DNA-dependent protein kinase activity is linked to V(D)J recombination and DNA repair defects associated with the murine sad mutation. Cell. 80:813-823.
8. Kirchgessner, C.U., C.K. Patil, J.W. Evans, C.A. Cuomo, L.M. Fried, T. Carter, M.A. Oettinger, and J.M. Brown. 1995. DNA-dependent kinase (p350) as a candidate gene for the murine SCID defect Science (Wash. DC). 267:1178-1182.
9. Rathmell, W.K., and G. Chu. 1994. Involvement of the Ku autoantigen in the cellular response to DNA double-strand breaks. Proc. Natl. Acad. Sci. USA. 91:7623-7627.
10. Taccioli, G.E., T.M. Gottlieb, T. Blunt, A. Priestley, J. Demengeot, R. Mizuta, A.R. Lehmann, F.W. Alt, S.P.Jackson, and P.A. Jeggo. 1994. Ku80. product of the XRCC5 gene and its role in DNA repair and V(D)J recombination. Science (Wash. DC). 265:1442-1445.
11. Smider, V., W.K. Rathmell, M.R. Lieber, and G. Chu. 1994. Restoration of X-ray resistance and V(D)J recombination in mutant cells by Ku cDNA. Science (Wash. DC). 266: 288-291.
12. Yancopoulos, G.D., and F.W. Alt. 1986. Regulation of the assembly and expression of variable-region genes. Annu. Rev. Immunol. 4:339-368.
13. Fondell, J.D., and K.B. Marcu. 1992. Transcription of germ line Vα segments correlates with ongoing T-cell receptor α-chain rearrangement. Mol. Cell. Biol. 12:1480-1489.
14. Schlissel, M.S., and D. Baltimore. 1989. Activation of immunoglobulin κ gene rearrangement correlates with induction of germline κ gene transcription. Cell. 58:1001-1007.
15. Grawunder, U., F. Melchers, and A. Rolink. 1995. Induction of sterile transcription from the KL chain gene locus in V(D)J-recombinase deficient progenitor B cells. Int. Immunol. 7:1915-1925.
16. Capone, M., F. Watrin, C. Fernex, B. Horvat, B. Krippl, L. Wu, R. Scollay, and P. Ferrier. 1993. TCRβ and TCRα gene enhancers confer tissue- and stage-specificity on V(D)J recombination events. EMBO (Eur. Mol. Biol. Organ.) J. 12: 4335-4346.
17. Takeda, S., Y.R. Zou, H. Bluethmann, D. Kitamura, U. Muller, and K. Rajewsky. 1993. Deletion of the immunoglobulin κ chain intron enhancer abolishes K chain gene rearrangements in cis but not λ chain rearrangements in trans. EMBO (Eur. Mol. Biol. Organ.) J. 12:2329-2336.
18. Lin, W.C., and S. Desideno. 1994. Cell cycle regulation of V(D)J recombination-activating protein RAG-2. Proc. Natl. Acad. Sci. USA. 91:2733-2737.
19. Lin, W.C., and S. Desiderio. 1993. Regulation of V(D)J recombination activator protein RAG-2 by phosphorylation. Science (Wash. DC). 260:953-959.
20. Rolink, A., A. Kudo, H. Karasuyama, Y. Kikuchi, and F. Melchers. 1991. Long-term proliferating early preB cell lines and clones with the potential to develop to surface-Ig positive mitogen-reactive B cells "in vitro" and "in vivo." EMBO (Eur. MoL. Biol. Organ.) J. 10:327-336.
21. Melchers, F., D. Haasner, U. Grawunder, C. Kalberer, H. Karasuyama, T. Winkler, and A. Rolink. 1994. Roles of IgH and L chains and of surrogate H and L chains in the development of cells of the B lymphocyte lineage. Annu. Rev. Immunol. 12:209-225.
22. Strasser, A., A.W. Harns, and S. Cory. 1991. bcl-2 transgene inhibits T cell death and perturbs thymic self-censorship. Cell. 67:889-899.
23. Strasser, A , S. Wittingham, D.L. Vaux, M.L. Bath, J.M. Adams, S. Cory, and A.W. Harris. 1991. Enforced BCL2 expression in B-lymphoid cells prolongs antibody responses and elicits autoimmune disease. Proc. Natl. Acad. Sci. USA. 88: 8661-8665.
24. + B cells can continue to rearrange κand λ L chain gene loci. J. Exp. Med. 178:1263-1270.
25. Ogawa, M., S. Nishikawa, K. Ikuta, F. Yamamura, M. Naito, K. Takahashi, and S.I. Nishikawa. 1988. B cell ontogeny in murine embryo studied by a culture system with the monolayer of a stromal cell clone, ST-2: B cell progenitor develops first in the embryonal body rather than the yolk sac. EMBO (Eur. Mol. Biol. Organ.) J. 7:1337-1343.
26. Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidimum thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
27. Bruggemann, E.P., V. Chaudhary, M.M. Gottesman, and I. Pastan. 1991. Pseudomonas exotoxin fusion proteins are potent immunogens for raising antibodies against P-glycoprotein. Biotechniques. 10:202-209.
28. Harlow, E., and D. Lane, editors. 1988 Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY. pp. 423-470.
29. Grawunder, U., T.M.J. Leu, D.G. Schatz, A. Werner, A.G. Rolink, F. Melchers, and T.H. Winkler. 1995. Shutdown of expression of RAG-1 and RAG-2 in preB cells after functional immunoglobulin μ-heavy chain rearrangement. Immunity. 3:601-608.
30. Rolink, A., U. Grawunder, T.H. Winkler, H. Karasuyama, and F. Melchers. 1994. IL-2 receptor α chain (CD25,TAC) expression defines a crucial stage in preB cell development. Int. Immunol. 6:1257-1264.
31. van Gent, D.C., J.F. McBlane, D.A. Ramsden, M.J. Sadofsky, J.E. Hesse, and M. Gellert. 1995. Initiation of V(D)J recombination in a cell-free system. Cell. 81:925-934.
32. Chen, Y.Y., L.C. Wang, M.S. Huang, and N. Rosenberg. 1994. An active v-abl protein tyrosine kinase blocks immunoglobulin light-chain gene rearrangement. Genes & Dev. 8: 688-697.
33. Klug, C.A., S.J. Gerety, P.C. Shah, Y.Y. Chen, N.R. Rice, N. Rosenberg, and H. Singh. 1994. The v-abl tyrosine kinase negatively regulates NB-κB/Rel factors and blocks K gene transcription in pre-B lymphocytes. Genes & Dev. 8:678-687.
34. Leu, T.M.J., and D.G. Schatz. 1995. Rag-1 and Rag-2 proteins are found in the same high molecular weight complex, with Rag-1 superimposing its physical properties on Rag-2. Mol. Cell Biol. 15:5657-5670.
35. Cuomo, C.A., S.A. Kirch, J. Gyuns, R. Brent, and M.A. Oettinger. 1994. Rch-1, a protein that specifically interacts with the RAG-1 recombination-activating protein. Proc. Natl. Acad. Sci. USA. 91:6156-6160.
36. Cortes, P., Z.S. Ye, and D. Baltimore, 1994. RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1. Proc. Natl. Acad. Sci. USA. 91:7633-7637.