A unitary non-NMDA receptor short subunit from Xenopus: DNA cloning and expression. 1996

H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
Molecular Neurobiology Unit, Royal Free Hospital School of Medicine, London, UK.

A high-affinity homomeric, non-NMDA glutamate receptor was previously purified from the amphibian Xenopus laevis. We have obtained nine peptide sequences from its subunit, applied in cDNA cloning. The cDNA encodes a subunit (XenU1) containing all nine sequences. The 51,600-dalton mature subunit has four hydrophobic domains homologous to the four in the C-terminal half of mammalian non-NMDA receptor subunits. Transient expression in COS cells showed 1:1 binding (at Bmax) of [3H] kainate (KD = 9.1 nM) and of [3H] AMPA (alpha-amino-3-hydroxy-5-methyl-isoxazole-4-propionic acid; KD = 62 nM). The competitive binding series domoate > kainate > AMPA > NBQX > glutamate was established (where NBQX is 2,3-dihydroxy-6-nitro-7-sulphamoyl-benzo (f) quinoxaline). Each agonist shows the same KI value against [3H] kainate and [3H] AMPA binding, suggesting a common agonist site, but two conformations thereof are distinguishable by their different affinities for the antagonist NBQX and by the allosteric effect of thiocyanate anion (greatly potentiating AMPA binding, inert with kainate). XenU1 is exceptional among non-NMDA receptor subunits because it lacks most of the large N-terminal domain found in those of mammals and it has high affinity for both kainate and AMPA. It differs from the similarly-short "kainate-binding proteins" (KBPs), in binding AMPA and in forming glutamate receptor channels when the native protein is reconstituted. Moreover, whereas a full-length kainate receptor of mammals, GluR6, is shown here (from a partial cDNA sequence) to exist also in Xenopus, with approximately 97% sequence identity to rat GluR6, XenU1 is much less homologous to any rat kainate or AMPA receptor and also to the KBPs, even from another amphibian, Rana. Another difference is that a potential concensus sequence ("EF hand") for Ca2+ binding is present in the N-terminal domain of XenU1, but not in the chicken (glial) KBP. XenU1 is deduced to be in a new family of non-NMDA receptors.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010442 Peptide Chain Initiation, Translational A process of GENETIC TRANSLATION whereby the formation of a peptide chain is started. It includes assembly of the RIBOSOME components, the MESSENGER RNA coding for the polypeptide to be made, INITIATOR TRNA, and PEPTIDE INITIATION FACTORS; and placement of the first amino acid in the peptide chain. The details and components of this process are unique for prokaryotic protein biosynthesis and eukaryotic protein biosynthesis. Chain Initiation, Peptide, Translational,Protein Biosynthesis Initiation,Protein Chain Initiation, Translational,Protein Translation Initiation,Translation Initiation, Genetic,Translation Initiation, Protein,Translational Initiation, Protein,Translational Peptide Chain Initiation,Biosynthesis Initiation, Protein,Genetic Translation Initiation,Initiation, Genetic Translation,Initiation, Protein Biosynthesis,Initiation, Protein Translation,Initiation, Protein Translational,Protein Translational Initiation
D011810 Quinoxalines Quinoxaline
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D002522 Chlorocebus aethiops A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research. African Green Monkey,Cercopithecus aethiops,Cercopithecus griseoviridis,Cercopithecus griseus,Cercopithecus pygerythrus,Cercopithecus sabeus,Cercopithecus tantalus,Chlorocebus cynosuros,Chlorocebus cynosurus,Chlorocebus pygerythrus,Green Monkey,Grivet Monkey,Lasiopyga weidholzi,Malbrouck,Malbrouck Monkey,Monkey, African Green,Monkey, Green,Monkey, Grivet,Monkey, Vervet,Savanah Monkey,Vervet Monkey,Savannah Monkey,African Green Monkey,Chlorocebus cynosuro,Green Monkey, African,Green Monkeys,Grivet Monkeys,Malbrouck Monkeys,Malbroucks,Monkey, Malbrouck,Monkey, Savanah,Monkey, Savannah,Savannah Monkeys,Vervet Monkeys
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
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

Related Publications

H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
March 1992, FEBS letters,
H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
January 1995, Receptors & channels,
H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
November 1992, FEBS letters,
H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
December 2000, Biochimica et biophysica acta,
H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
August 1998, Experimental eye research,
H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
March 2005, Neuroscience letters,
H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
June 2005, Brain research. Molecular brain research,
H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
October 1997, Journal of molecular biology,
H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
June 1994, Proceedings of the National Academy of Sciences of the United States of America,
H Ishimaru, and R Kamboj, and A Ambrosini, and J M Henley, and M M Soloviev, and H Sudan, and J Rossier, and K Abutidze, and V Rampersad, and P N Usherwood, and A N Bateson, and E A Barnard
April 2002, Brain research. Molecular brain research,
Copied contents to your clipboard!