Molecular cloning and nucleotide sequence of rat kidney gamma-glutamyl transpeptidase cDNA. 1986

Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën

We have screened a cDNA library (20,000 clones) made from rat kidney poly(A)+ RNA, using an oligonucleotide probe that was a mixture of 14-base DNA oligomers containing all 32 possible sequences coding for residues 32-36 of the gamma-glutamyl transpeptidase (EC 2.3.2.2.) heavy chain. We isolated and sequenced two cDNAs corresponding to the mRNA coding for the entire length of the enzyme precursor. The nucleotide sequence that we obtained (2072 bases) reveals an open reading frame of 1707 nucleotides coding for the common precursor of both enzyme subunits. The amino acid sequence begins with the 21 residues located at the NH2-terminal hydrophobic region of the heavy subunit. We show that this sequence, which is not processed, is the only possible signal peptide in the sequence. Five potential N-glycosylation sites are present in the gamma-glutamyl transpeptidase sequence. Using one of the two cDNA clones as probe, a 2.2-kilobase sequence was detected by blot analysis in rat kidney and human fetal liver RNA.

UI MeSH Term Description Entries
D007668 Kidney Body organ that filters blood for the secretion of URINE and that regulates ion concentrations. Kidneys
D011061 Poly A A group of adenine ribonucleotides in which the phosphate residues of each adenine ribonucleotide act as bridges in forming diester linkages between the ribose moieties. Adenine Polynucleotides,Polyadenylic Acids,Poly(rA),Polynucleotides, Adenine
D011498 Protein Precursors Precursors, Protein
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D004274 DNA, Recombinant Biologically active DNA which has been formed by the in vitro joining of segments of DNA from different sources. It includes the recombination joint or edge of a heteroduplex region where two recombining DNA molecules are connected. Genes, Spliced,Recombinant DNA,Spliced Gene,Recombinant DNA Research,Recombination Joint,DNA Research, Recombinant,Gene, Spliced,Joint, Recombination,Research, Recombinant DNA,Spliced Genes
D005723 gamma-Glutamyltransferase An enzyme, sometimes called GGT, with a key role in the synthesis and degradation of GLUTATHIONE; (GSH, a tripeptide that protects cells from many toxins). It catalyzes the transfer of the gamma-glutamyl moiety to an acceptor amino acid. GGTP,Glutamyl Transpeptidase,gammaglutamyltransferase,gamma-Glutamyl Transpeptidase,Transpeptidase, Glutamyl,Transpeptidase, gamma-Glutamyl,gamma Glutamyl Transpeptidase,gamma Glutamyltransferase
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA

Related Publications

Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën
December 1988, Proceedings of the National Academy of Sciences of the United States of America,
Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën
March 1977, European journal of biochemistry,
Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën
August 1990, The Journal of biological chemistry,
Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën
March 1985, Nucleic acids research,
Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën
January 1985, Methods in enzymology,
Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën
March 1989, Gene,
Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën
September 1981, Archives internationales de physiologie et de biochimie,
Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën
December 1995, Gene,
Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën
January 1986, Nucleic acids symposium series,
Y Laperche, and F Bulle, and T Aissani, and M N Chobert, and M Aggerbeck, and J Hanoune, and G Guellaën
January 1984, The Journal of biological chemistry,
Copied contents to your clipboard!