The putative glutamate receptor 3.2 from Arabidopsis thaliana (AtGLR3.2) is an integral membrane peptide that accumulates in rapidly growing tissues and persists in vascular-associated tissues

Plant Science

Volumn 163, Issue 1, 2002, Pages 43-51

  Turano, Frank J ^a   Muhitch, Michael J ^b   Felker, Frederick C ^b   McMahon, Michael B ^c  

^a GEORGE WASHINGTON UNIVERSITY   (United States)

^b NATIONAL CENTER FOR AGRICULTURAL UTILIZATION RESEARCH   (United States)

^c USDA ARS Foreign Disease Weed Science Research Unit   (United States)

Author keywords

Arabidopsis; Gene expression; Putative glutamate receptor; Tissue localization

Indexed keywords

GENES; MOLECULAR WEIGHT; RNA; SEED; TISSUE;

IMMUNOHISTOCHEMICAL STAINING;

POLYPEPTIDES;

GENES; MOLECULAR WEIGHT; NUCLEIC ACIDS; PEPTIDES; SEEDS; TISSUE;

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 0036664573     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(02)00057-2     Document Type: Article

References (12)

1. H.-M. Lam, J. Chiu, M.-H. Hsieh, L. Meisel, I.C. Oliveira, M. Shin, G.M. Coruzzi, Glutamate-receptor genes in plants, Nature 396 (1998) 125-126.
2. B. Lacombe, D. Becker, R. Hedrich, R. DeSalle, M. Hollmann, J.M. Kwak, J.I. Schroeder, N. Le Novere, H.-G. Nam, E.P. Spalding, M. Tester, F.J. Turano, J. Chiu, G.M. Coruzzi, On the identity of plant glutamate receptors, Science 292 (2001) 1486-1487.
3. E.D. Brenner, N. Martinez-Barboza, A.P. Clark, Q.S. Liang, D.W. Stevenson, G.M. Coruzzi, Arabidopsis mutants resistant to S(+)-beta-methyl-alpha, beta-diaminopropionic acid, a cycadderived glutamate receptor agonist, Plant Physiol. 124 (2000) 1615-1624.
4. S.A. Kim, J.M. Kwak, S.K. Jae, M.H. Wang, H.G. Nam, Overexpression of the AtGluR2 gene encoding an Arabidopsis homolog of mammalian glutamate receptors impairs calcium utilization and sensitivity to ionic stress in transgenic plants, Plant Cell Physiol. 42 (2001) 74-84.
5. K.L. Dennison, E.P. Spalding, Glutamate-gated calcium fluxes in Arabidopsis, Plant Physiol. 124 (2000) 1511-1514.
6. J. Chiu, R. DeSalle, H.-M. Lam, L. Meisel, G.M. Coruzzi, Molecular evolution of glutamate receptors: a primitive signaling mechanism that existed before plants and animais diverged, Mol. Biol. Evol. 16 (1999) 826-838.
7. F.J. Turano, J.M. Weisemann, B.F. Matthews, Identification and expression of a cDNA clone encoding aspartate aminotransferase in carrot, Plant Physiol. 100 (1992) 374-381.
8. F.J. Turano, M.J. Muhitch, Differential accumulation of ferredoxin- and NADH-dependent glutamate synthase activities, peptides, and transcripts in developing soybean seedlings in -response to light, nitrogen, and nodulation, Physiol. Plant 107 (1999) 407-418.
9. M.D. Marks, J. West, D.P. Weeks, The relatively large beta-tubulin gene family of Arabidopsis contains a member with ah unusual transcribed 5′ noncoding sequence, Plant Mol. Biol. 10 (1987) 91-104.
10. I. Unfried, U. Strocker, P. Gruendler, Nucleotide sequence of the 18S rRNA gene from Arabidopsis thaliana Col0, Nucleic Acids Res. 17 (1989) 7513-7515.
11. A. Koff, A. Giordano, D. Desai, K. Yamashita, J.W. Harper, S. Elledge, T. Nishimoto, D.O. Morgan, B.R. Franza, J.M. Roberts, Formation and activation of a cyclin E-cdk2 complex during the G1 phase of the human cell cycle, Science 257 (1992) 1689-1694.
12. F.J. Turano, G.R. Panta, M.W. Allard, P. van Berkum, The putative glutamate receptors from plants are related to two superfamilies of animal neurotransmitter receptors via distinct evolutionary mechanisms, Mol. Biol. Evol. 18 (2001) 1417-1420.