Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 May;78(5):2772–2776. doi: 10.1073/pnas.78.5.2772

cDNA clone coding for part of a mouse H-2d major histocompatibility antigen.

S Kvist, F Bregegere, L Rask, B Cami, H Garoff, F Daniel, K Wiman, D Larhammar, J P Abastado, G Gachelin, P A Peterson, B Dobberstein, P Kourilsky
PMCID: PMC319439  PMID: 6265910

Abstract

mRNA coding for mouse major transplantation antigens of the d haplotype was partially purified, copied into double-stranded cDNA, and cloned in Escherichia coli. Clones were selected by their ability to hybridize specifically with mRNA coding for H-2K, D, or L antigens. One of these clones, pH-2d-1, carries a 1200-base-pair insert, comprising the noncoding region, including poly(A) at the 3' end and part of the coding region. A partial sequence of the latter region showed extensive homology with the known amino acid sequences of H-2Kb,Kk, and HLA-B7 antigens. From this comparison, it appears that the coding region extends from amino acid 133 in the second domain, through the third domain, to the cytoplasmic COOH-terminal region. A stretch of 24 hydrophobic or uncharged residues, located 31 amino acids from the COOH-terminal end, could represent the segment that spans the membrane. This is followed on the cytoplasmic side of the membrane by a cluster of basic amino acids and a possible phosphorylation site on a threonine residue.

Full text

PDF
2772

Images in this article

2773Image
on p.2773

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Auffray C., Nageotte R., Chambraud B., Rougeon F. Mouse immunoglobulin genes: a bacterial plasmid containing the entire coding sequence for a pre-gamma 2a heavy chain. Nucleic Acids Res. 1980 Mar 25;8(6):1231–1241. doi: 10.1093/nar/8.6.1231. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1408–1412. doi: 10.1073/pnas.69.6.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bastia D. Determination of restriction sites and the nucleotide sequence surrounding the relaxation site of ColE1. J Mol Biol. 1978 Oct 5;124(4):601–639. doi: 10.1016/0022-2836(78)90174-2. [DOI] [PubMed] [Google Scholar]
  4. Blobel G., Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol. 1975 Dec;67(3):835–851. doi: 10.1083/jcb.67.3.835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bolivar F., Rodriguez R. L., Greene P. J., Betlach M. C., Heyneker H. L., Boyer H. W., Crosa J. H., Falkow S. Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene. 1977;2(2):95–113. [PubMed] [Google Scholar]
  6. Coligan J. E., Kindt T. J., Ewenstein B. M., Uehara H., Martinko J. M., Nathenson S. G. Further structural analysis of the murine H-2Kb glycoprotein using radiochemical methodology. Mol Immunol. 1979 Jan;16(1):3–8. doi: 10.1016/0161-5890(79)90021-x. [DOI] [PubMed] [Google Scholar]
  7. Coligan J. E., Kindt T. J., Nairn R., Nathenson S. G., Sachs D. H., Hansen T. H. Primary structural studies of an H-2L molecule confirm that it is a unique gene product with homology to H-2K and H-2D antigens. Proc Natl Acad Sci U S A. 1980 Feb;77(2):1134–1138. doi: 10.1073/pnas.77.2.1134. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dobberstein B., Garoff H., Warren G., Robinson P. J. Cell-free synthesis and membrane insertion of mouse H-2Dd histocompatibility antigen and beta 2-microglobulin. Cell. 1979 Aug;17(4):759–769. doi: 10.1016/0092-8674(79)90316-7. [DOI] [PubMed] [Google Scholar]
  9. Garoff H., Frischauf A. M., Simons K., Lehrach H., Delius H. Nucleotide sequence of cdna coding for Semliki Forest virus membrane glycoproteins. Nature. 1980 Nov 20;288(5788):236–241. doi: 10.1038/288236a0. [DOI] [PubMed] [Google Scholar]
  10. Garoff H., Simons K., Dobberstein B. Assembly of the Semliki Forest virus membrane glycoproteins in the membrane of the endoplasmic reticulum in vitro. J Mol Biol. 1978 Oct 5;124(4):587–600. doi: 10.1016/0022-2836(78)90173-0. [DOI] [PubMed] [Google Scholar]
  11. Grunstein M., Hogness D. S. Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3961–3965. doi: 10.1073/pnas.72.10.3961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kimball E. S., Maloy W. L., Martinko J. M., Nathenson S. G., Coligan J. E. Structural studies on H-2Db and H-2Kd molecules indicate that murine major histocompatibility b and d haplotype alloantigens share structural features. Mol Immunol. 1980 Oct;17(10):1283–1291. doi: 10.1016/0161-5890(80)90025-5. [DOI] [PubMed] [Google Scholar]
  13. Klein J. The major histocompatibility complex of the mouse. Science. 1979 Feb 9;203(4380):516–521. doi: 10.1126/science.104386. [DOI] [PubMed] [Google Scholar]
  14. Kvist S., Ostberg L., Peterson P. A. Reactions and crossreactions of a rabbit anti-H2 antigen serum. Scand J Immunol. 1978 Apr;7(4):265–276. doi: 10.1111/j.1365-3083.1978.tb00454.x. [DOI] [PubMed] [Google Scholar]
  15. Marshall R. D. Glycoproteins. Annu Rev Biochem. 1972;41:673–702. doi: 10.1146/annurev.bi.41.070172.003325. [DOI] [PubMed] [Google Scholar]
  16. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  17. Monahan J. J., McReynolds L. A., O'Malley B. W. The ovalbumin gene. In vitro enzymatic synthesis and characterization. J Biol Chem. 1976 Dec 10;251(23):7355–7362. [PubMed] [Google Scholar]
  18. Murray N. E., Brammar W. J., Murray K. Lambdoid phages that simplify the recovery of in vitro recombinants. Mol Gen Genet. 1977 Jan 7;150(1):53–61. doi: 10.1007/BF02425325. [DOI] [PubMed] [Google Scholar]
  19. Myers J. C., Spiegelman S. Sodium pyrophosphate inhibition of RNA.DNA hybrid degradation by reverse transcriptase. Proc Natl Acad Sci U S A. 1978 Nov;75(11):5329–5333. doi: 10.1073/pnas.75.11.5329. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Nathenson S. G., Cullen S. E. Biochemical properties and immunochemical-genetic relationships of mouse H-2 alloantigens. Biochim Biophys Acta. 1974 Apr 8;344(1):1–25. doi: 10.1016/0304-4157(74)90006-9. [DOI] [PubMed] [Google Scholar]
  21. Orr H. T., López de Castro J. A., Lancet D., Strominger J. L. Complete amino acid sequence of a papain-solubilized human histocompatibility antigen, HLA-B7. 2. Sequence determination and search for homologies. Biochemistry. 1979 Dec 11;18(25):5711–5720. doi: 10.1021/bi00592a030. [DOI] [PubMed] [Google Scholar]
  22. Ploegh H. L., Orr H. T., Strominger J. L. Molecular cloning of a human histocompatibility antigen cDNA fragment. Proc Natl Acad Sci U S A. 1980 Oct;77(10):6081–6085. doi: 10.1073/pnas.77.10.6081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Pober J. S., Guild B. C., Strominger J. L. Phosphorylation in vivo and in vitro of human histocompatibility antigens (HLA-A and HLA-B) in the carboxy-terminal intracellular domain. Proc Natl Acad Sci U S A. 1978 Dec;75(12):6002–6006. doi: 10.1073/pnas.75.12.6002. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Rask L., Wålinder O., Zetterqvist O., Engström L. Protein-bound phosphorylthreonine in some tissues and organisms. Biochim Biophys Acta. 1970 Oct 20;221(1):107–113. doi: 10.1016/0005-2795(70)90201-1. [DOI] [PubMed] [Google Scholar]
  25. Ricciardi R. P., Miller J. S., Roberts B. E. Purification and mapping of specific mRNAs by hybridization-selection and cell-free translation. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4927–4931. doi: 10.1073/pnas.76.10.4927. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Robb R. J., Terhorst C., Strominger J. L. Sequence of the COOH-terminal hydrophilic region of histocompatibility antigens HLA-A2 and HLA-B7. J Biol Chem. 1978 Aug 10;253(15):5319–5324. [PubMed] [Google Scholar]
  27. Rothbard J. B., Hopp T. P., Edelman G. M., Cunningham B. A. Structure of the heavy chain of the H-2Kk histocompatibility antigen. Proc Natl Acad Sci U S A. 1980 Jul;77(7):4239–4243. doi: 10.1073/pnas.77.7.4239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Rougeon F., Kourilsky P., Mach B. Insertion of a rabbit beta-globin gene sequence into an E. coli plasmid. Nucleic Acids Res. 1975 Dec;2(12):2365–2378. doi: 10.1093/nar/2.12.2365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Rougeon F., Mach B. Cloning and amplification of rabbit alpha- and beta-globin gene sequences into Escherichia coli plasmids. J Biol Chem. 1977 Apr 10;252(7):2209–2217. [PubMed] [Google Scholar]
  30. Smith H. O., Birnstiel M. L. A simple method for DNA restriction site mapping. Nucleic Acids Res. 1976 Sep;3(9):2387–2398. doi: 10.1093/nar/3.9.2387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Tabak H. F., Flavell R. A. A method for the recovery of DNA from agarose gels. Nucleic Acids Res. 1978 Jul;5(7):2321–2332. doi: 10.1093/nar/5.7.2321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Uehara H., Ewenstein B. M., Martinko J. M., Nathenson S. G., Coligan J. E., Kindt T. J. Primary structure of murine major histocompatibility complex alloantigens: amino acid sequence of the amino-terminal one hundred and seventy-three residues of the H-2Kb glycoprotein. Biochemistry. 1980 Jan 22;19(2):306–315. doi: 10.1021/bi00543a009. [DOI] [PubMed] [Google Scholar]
  33. Villa-Komaroff L., Efstratiadis A., Broome S., Lomedico P., Tizard R., Naber S. P., Chick W. L., Gilbert W. A bacterial clone synthesizing proinsulin. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3727–3731. doi: 10.1073/pnas.75.8.3727. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Vitetta E. S., Capra J. D. The protein products of the murine 17th chromosome: genetics and structure. Adv Immunol. 1978;26:147–193. doi: 10.1016/s0065-2776(08)60230-8. [DOI] [PubMed] [Google Scholar]
  35. Walsh F. S., Crumpton M. J. Orientation of cell-surface antigens in the lipid bilayer of lymphocyte plasma membrane. Nature. 1977 Sep 22;269(5626):307–311. doi: 10.1038/269307a0. [DOI] [PubMed] [Google Scholar]
  36. Yeaman S. J., Cohen P., Watson D. C., Dixon G. H. The substrate specificity of adenosine 3':5'-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle. Biochem J. 1977 Feb 15;162(2):411–421. doi: 10.1042/bj1620411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Zetterqvist O., Ragnarsson U., Humble E., Berglund L., Engström L. The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver. Biochem Biophys Res Commun. 1976 Jun 7;70(3):696–703. doi: 10.1016/0006-291x(76)90648-3. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES