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Cloning and characterization of human and rat liver cDNAs coding for a gap junction protein.

The Journal of Cell Biology, 01 Sep 1986, 103(3):767-776
https://doi.org/10.1083/jcb.103.3.767 PMID: 2875078 PMCID: PMC2114303

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Abstract 

An extended synthetic oligonucleotide (58-mer) has been used to identify and characterize a human liver gap junction cDNA. The cDNA is 1,574 bases long and contains the entire coding region for a gap junction protein. In vitro translation of the RNA products of this cDNA is consistent with it coding for a 32,022-D protein. Southern blot analysis indicates that the gap junction gene is present as a single copy, and that it can be detected in a variety of organisms using the human liver cDNA as a probe. The human cDNA has been used to screen a rat liver cDNA library, and a rat liver junction cDNA clone has been isolated. The rat liver clone is 1,127 bases in length, and it has strong sequence homology to the human cDNA in the protein-coding region, but less extensive homology in the 3'-untranslated region.

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J Cell Biol. 1986 Sep 1; 103(3): 767–776.
PMCID: PMC2114303
PMID: 2875078

Cloning and characterization of human and rat liver cDNAs coding for a gap junction protein

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Abstract

An extended synthetic oligonucleotide (58-mer) has been used to identify and characterize a human liver gap junction cDNA. The cDNA is 1,574 bases long and contains the entire coding region for a gap junction protein. In vitro translation of the RNA products of this cDNA is consistent with it coding for a 32,022-D protein. Southern blot analysis indicates that the gap junction gene is present as a single copy, and that it can be detected in a variety of organisms using the human liver cDNA as a probe. The human cDNA has been used to screen a rat liver cDNA library, and a rat liver junction cDNA clone has been isolated. The rat liver clone is 1,127 bases in length, and it has strong sequence homology to the human cDNA in the protein-coding region, but less extensive homology in the 3'-untranslated region.

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Selected References

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  • Paul DL. Molecular cloning of cDNA for rat liver gap junction protein. J Cell Biol. 1986 Jul;103(1):123–134. [Europe PMC free article] [Abstract] [Google Scholar]
  • Atkinson MM, Menko AS, Johnson RG, Sheppard JR, Sheridan JD. Rapid and reversible reduction of junctional permeability in cells infected with a temperature-sensitive mutant of avian sarcoma virus. J Cell Biol. 1981 Nov;91(2 Pt 1):573–578. [Europe PMC free article] [Abstract] [Google Scholar]
  • Auffray C, Rougeon F. Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA. Eur J Biochem. 1980 Jun;107(2):303–314. [Abstract] [Google Scholar]
  • Azarnia R, Loewenstein WR. Intercellular communication and the control of growth: X. Alteration of junctional permeability by the src gene. A study with temperature-sensitive mutant Rous sarcoma virus. J Membr Biol. 1984;82(3):191–205. [Abstract] [Google Scholar]
  • Biggin MD, Gibson TJ, Hong GF. Buffer gradient gels and 35S label as an aid to rapid DNA sequence determination. Proc Natl Acad Sci U S A. 1983 Jul;80(13):3963–3965. [Europe PMC free article] [Abstract] [Google Scholar]
  • Dale RM, McClure BA, Houchins JP. A rapid single-stranded cloning strategy for producing a sequential series of overlapping clones for use in DNA sequencing: application to sequencing the corn mitochondrial 18 S rDNA. Plasmid. 1985 Jan;13(1):31–40. [Abstract] [Google Scholar]
  • Dermietzel R, Leibstein A, Frixen U, Janssen-Timmen U, Traub O, Willecke K. Gap junctions in several tissues share antigenic determinants with liver gap junctions. EMBO J. 1984 Oct;3(10):2261–2270. [Europe PMC free article] [Abstract] [Google Scholar]
  • Dreyfuss G, Adam SA, Choi YD. Physical change in cytoplasmic messenger ribonucleoproteins in cells treated with inhibitors of mRNA transcription. Mol Cell Biol. 1984 Mar;4(3):415–423. [Europe PMC free article] [Abstract] [Google Scholar]
  • Ehrhart JC, Chauveau J. The protein component of mouse hepatocyte gap junctions. FEBS Lett. 1977 Jun 15;78(2):295–299. [Abstract] [Google Scholar]
  • Epstein ML, Gilula NB. A study of communication specificity between cells in culture. J Cell Biol. 1977 Dec;75(3):769–787. [Europe PMC free article] [Abstract] [Google Scholar]
  • Feinberg AP, Vogelstein B. "A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity". Addendum. Anal Biochem. 1984 Feb;137(1):266–267. [Abstract] [Google Scholar]
  • Finbow M, Yancey SB, Johnson R, Revel JP. Independent lines of evidence suggesting a major gap junctional protein with a molecular weight of 26,000. Proc Natl Acad Sci U S A. 1980 Feb;77(2):970–974. [Europe PMC free article] [Abstract] [Google Scholar]
  • Finbow ME, Shuttleworth J, Hamilton AE, Pitts JD. Analysis of vertebrate gap junction protein. EMBO J. 1983;2(9):1479–1486. [Europe PMC free article] [Abstract] [Google Scholar]
  • Gilula NB, Reeves OR, Steinbach A. Metabolic coupling, ionic coupling and cell contacts. Nature. 1972 Feb 4;235(5336):262–265. [Abstract] [Google Scholar]
  • Grantham R, Gautier C, Gouy M, Jacobzone M, Mercier R. Codon catalog usage is a genome strategy modulated for gene expressivity. Nucleic Acids Res. 1981 Jan 10;9(1):r43–r74. [Europe PMC free article] [Abstract] [Google Scholar]
  • Gros DB, Nicholson BJ, Revel JP. Comparative analysis of the gap junction protein from rat heart and liver: is there a tissue specificity of gap junctions? Cell. 1983 Dec;35(2 Pt 1):539–549. [Abstract] [Google Scholar]
  • Henderson D, Eibl H, Weber K. Structure and biochemistry of mouse hepatic gap junctions. J Mol Biol. 1979 Aug 5;132(2):193–218. [Abstract] [Google Scholar]
  • Hertzberg EL. A detergent-independent procedure for the isolation of gap junctions from rat liver. J Biol Chem. 1984 Aug 10;259(15):9936–9943. [Abstract] [Google Scholar]
  • Hertzberg EL, Gilula NB. Isolation and characterization of gap junctions from rat liver. J Biol Chem. 1979 Mar 25;254(6):2138–2147. [Abstract] [Google Scholar]
  • Hertzberg EL, Skibbens RV. A protein homologous to the 27,000 dalton liver gap junction protein is present in a wide variety of species and tissues. Cell. 1984 Nov;39(1):61–69. [Abstract] [Google Scholar]
  • Hertzberg EL, Anderson DJ, Friedlander M, Gilula NB. Comparative analysis of the major polypeptides from liver gap junctions and lens fiber junctions. J Cell Biol. 1982 Jan;92(1):53–59. [Europe PMC free article] [Abstract] [Google Scholar]
  • Hertzberg EL, Spray DC, Bennett MV. Reduction of gap junctional conductance by microinjection of antibodies against the 27-kDa liver gap junction polypeptide. Proc Natl Acad Sci U S A. 1985 Apr;82(8):2412–2416. [Europe PMC free article] [Abstract] [Google Scholar]
  • Hubbard SC, Ivatt RJ. Synthesis and processing of asparagine-linked oligosaccharides. Annu Rev Biochem. 1981;50:555–583. [Abstract] [Google Scholar]
  • Konarska MM, Padgett RA, Sharp PA. Recognition of cap structure in splicing in vitro of mRNA precursors. Cell. 1984 Oct;38(3):731–736. [Abstract] [Google Scholar]
  • Kozak M. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 1984 Jan 25;12(2):857–872. [Europe PMC free article] [Abstract] [Google Scholar]
  • Kozak M. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell. 1986 Jan 31;44(2):283–292. [Abstract] [Google Scholar]
  • Krebs EG, Beavo JA. Phosphorylation-dephosphorylation of enzymes. Annu Rev Biochem. 1979;48:923–959. [Abstract] [Google Scholar]
  • Kwok SC, Ledley FD, DiLella AG, Robson KJ, Woo SL. Nucleotide sequence of a full-length complementary DNA clone and amino acid sequence of human phenylalanine hydroxylase. Biochemistry. 1985 Jan 29;24(3):556–561. [Abstract] [Google Scholar]
  • Langridge J, Langridge P, Bergquist PL. Extraction of nucleic acids from agarose gels. Anal Biochem. 1980 Apr;103(2):264–271. [Abstract] [Google Scholar]
  • Lawrence TS, Beers WH, Gilula NB. Transmission of hormonal stimulation by cell-to-cell communication. Nature. 1978 Apr 6;272(5653):501–506. [Abstract] [Google Scholar]
  • Lo KM, Jones SS, Hackett NR, Khorana HG. Specific amino acid substitutions in bacterioopsin: Replacement of a restriction fragment in the structural gene by synthetic DNA fragments containing altered codons. Proc Natl Acad Sci U S A. 1984 Apr;81(8):2285–2289. [Europe PMC free article] [Abstract] [Google Scholar]
  • Makowski L, Caspar DL, Phillips WC, Goodenough DA. Gap junction structures. II. Analysis of the x-ray diffraction data. J Cell Biol. 1977 Aug;74(2):629–645. [Europe PMC free article] [Abstract] [Google Scholar]
  • Melton DA, Krieg PA, Rebagliati MR, Maniatis T, Zinn K, Green MR. Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 1984 Sep 25;12(18):7035–7056. [Europe PMC free article] [Abstract] [Google Scholar]
  • Michalke W, Loewenstein WR. Communication between cells of different type. Nature. 1971 Jul 9;232(5306):121–122. [Abstract] [Google Scholar]
  • Mohun TJ, Brennan S, Dathan N, Fairman S, Gurdon JB. Cell type-specific activation of actin genes in the early amphibian embryo. Nature. 1984 Oct 25;311(5988):716–721. [Abstract] [Google Scholar]
  • Nicholson BJ, Hunkapiller MW, Grim LB, Hood LE, Revel JP. Rat liver gap junction protein: properties and partial sequence. Proc Natl Acad Sci U S A. 1981 Dec;78(12):7594–7598. [Europe PMC free article] [Abstract] [Google Scholar]
  • Nicholson BJ, Takemoto LJ, Hunkapiller MW, Hood LE, Revel JP. Differences between liver gap junction protein and lens MIP 26 from rat: implications for tissue specificity of gap junctions. Cell. 1983 Mar;32(3):967–978. [Abstract] [Google Scholar]
  • Nicholson BJ, Gros DB, Kent SB, Hood LE, Revel JP. The Mr 28,000 gap junction proteins from rat heart and liver are different but related. J Biol Chem. 1985 Jun 10;260(11):6514–6517. [Abstract] [Google Scholar]
  • Patschinsky T, Hunter T, Esch FS, Cooper JA, Sefton BM. Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation. Proc Natl Acad Sci U S A. 1982 Feb;79(4):973–977. [Europe PMC free article] [Abstract] [Google Scholar]
  • Revel JP, Karnovsky MJ. Hexagonal array of subunits in intercellular junctions of the mouse heart and liver. J Cell Biol. 1967 Jun;33(3):C7–C12. [Europe PMC free article] [Abstract] [Google Scholar]
  • Saez JC, Spray DC, Nairn AC, Hertzberg E, Greengard P, Bennett MV. cAMP increases junctional conductance and stimulates phosphorylation of the 27-kDa principal gap junction polypeptide. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2473–2477. [Europe PMC free article] [Abstract] [Google Scholar]
  • Thomas PS. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. [Europe PMC free article] [Abstract] [Google Scholar]
  • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. [Europe PMC free article] [Abstract] [Google Scholar]
  • Ullrich A, Berman CH, Dull TJ, Gray A, Lee JM. Isolation of the human insulin-like growth factor I gene using a single synthetic DNA probe. EMBO J. 1984 Feb;3(2):361–364. [Europe PMC free article] [Abstract] [Google Scholar]
  • Unwin PN, Zampighi G. Structure of the junction between communicating cells. Nature. 1980 Feb 7;283(5747):545–549. [Abstract] [Google Scholar]
  • Warner AE, Guthrie SC, Gilula NB. Antibodies to gap-junctional protein selectively disrupt junctional communication in the early amphibian embryo. Nature. 1984 Sep 13;311(5982):127–131. [Abstract] [Google Scholar]
  • WEIDMANN S. The electrical constants of Purkinje fibres. J Physiol. 1952 Nov;118(3):348–360. [Abstract] [Google Scholar]
  • Wiener EC, Loewenstein WR. Correction of cell-cell communication defect by introduction of a protein kinase into mutant cells. Nature. 305(5933):433–435. [Abstract] [Google Scholar]
  • Zervos AS, Hope J, Evans WH. Preparation of a gap junction fraction from uteri of pregnant rats: the 28-kD polypeptides of uterus, liver, and heart gap junctions are homologous. J Cell Biol. 1985 Oct;101(4):1363–1370. [Europe PMC free article] [Abstract] [Google Scholar]
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