Glutamine synthetase genes

Inducibility of the glutamine synthetase gene family of Phaseolus vulgaris L. 

Cock, J.M., Brock, I.W., Watson, A.T., Swarup, R., Morby, A.P. Cullimore, J.V. (1991). Regulation of glutamine synthetase genes in leaves of Phaseolus vulgaris. Plant Molecular Biology 17, 761-71. 

Cock, J.M., Mould, R.M., Bennett, M.J. Cullimore, J.V. (1990). Expression of glutamine synthetase genes in roots and nodules of Phaseolus vulgaris following changes in the ammonium supply and infection with various Rhizobium mutants. Plant Molecular Biology 14, 549-60. 

Forde, B.G., Day, H.M., Turton, J.F., Shen, W.-J., Cullimore, J.V. Oliver, J.E. (1989). Two glutamine synthetase genes from Phaseolus vulgaris L. display contrasting developmental and spatial patterns of expression in transgenic Lotus corniculatus plants. The Plant Cell 1, 391-401. 

Forde, B.G., Freeman, J., Oliver, J.E. Pineda, M. (1990). Nuclear factors interact with conserved A/T-rich elements upstream of a nodule-enhanced glutamine synthetase gene from French bean. The Plant Cell 2, 925-39. 

Primary structure and differential expression of glutamine synthetase genes in nodules, roots and leaves of Phaseolus vulgaris. The EMBO Journal 5, 1429-35. 

Glutamine synthetase genes are regulated by ammonia provided externally or by symbiotic nitrogen fixation. The EMBO Journal 6, 1167-71. 

Tingey, S.V., Walker, E.L. Coruzzi, G.M. (1987). Glutamine synthetase genes of pea encode distinct polypeptides which are differentially expressed in leaves, roots and nodules. The EMBO Journal 6, 1-9. 

Gebhardt, C., Olivier, J.E., Forde, B.G., Saarelainen, R. Miflin, B.J. (1986). Primary structure and differential expression of glutamine synthetase genes in nodules, roots and leaves of Phaseolus vulgaris. The EMBO Journal 5, 1429-35. 

Hirel, B., Bouet, C., King, B., Layzell, D., Jacobs, F. Verma, D.P.S. (1987). Glutamine synthetase genes are regulated by ammonia provided externally or by symbiotic nitrogen fixation. The EM BO Journal 5, 1167-71. 

Sengupta-Gopalan, C. Pitas, J.W. (1986). Expression of nodule-specific glutamine synthetase genes during nodule development in soybeans. Plant Molecular Biology 7, 189-99. 

Bebbington CR, Renner G, Thomson S, King D, Abrams D, Yarranton GT (1992), High level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplifiable selectable marker, Biotechnology 10 169-175. 

Sanders PG, Wilson RH (1984), Amplification and cloning of the Chinese hamster glutamine synthetase gene, EMBO J. 3 65-71. 

Cockett, M.I., C.R. Bebbington, and G.T. Yarranton. 1990. High level expression of tissue inhibitor of metallopro-teinases in Chinese hamster ovary cel Is using glutamine synthetase gene amplification. Biotechnol (NY) 8 662-667. 

Chen, Q., and Silflow, C. D. (1996). Isolation and characterization of glutamine synthetase genes in Chlamydomonas reinhardtii. Plant Physiol 112, 987—996. 

Pesole, G., Bozzetti, M. P., Lanave, C., Preparata, G., and Saccone, C. (1991). Glutamine synthetase gene evolution—A good molecular clock. Proc. Natnl. Acad. Sci. USA. 88, 522—526. 

Takabayashi, M., Wilkerson, P. P., and Robertson, D. (2005). Response of glutamine synthetase gene transcription and enzyme activity to external nitrogen sources in the diatom Skeletonema costatum (BacUlariophyceae). J. Phycol. 41, 84-94. 

Turner, N. E., Robinson, S. J., and Haselkom, R. (1983). Different promoters for the Anabaena glutamine synthetase gene during growth using molecular or fixed nitrogen. Nature. 306, 337—342. 

Wyman, M. (1999). Diel rhythms in ribulose-l,5-bisphosphate carboxylase/oxygenase and glutamine synthetase gene expression in a natural population of marine picoplanktonic cyanobacteria Syne-chococais spp.). Appl. Environ. Microbiol. 65, 3651—3659. 

The next most commonly used cell lines are the murine myeloma cell lines such as NS(T and Sp2/0. The NSO cell line is deficient for the glutamine synthetase gene, and the presence of glutamine synthetase (GS) gene on vectors has been used for the selection of stably integrated expression cassettes. ... 

Cockett, M.L, Bebbington, C.R., and Yarranton, G.T., High level expression of tissue inhibitor of metalloproteinases in Chinese hamster ovary cells using glutamine synthetase gene amphfication. Biotechnology (NY), 8, 662, 1990. 

Patejunas, G. Young, AP. (1990). Constitutive and glucocorticoid-mediated activation of glutamine synthetase gene expression in developing chicken retina. J. Biol. Chan., 265, 15280-5. 

Zhang, H.-Y. Young, A.P. (1991). A single upstream glucocorticoid response element juxtaposed to an APl/ATF/ CRE-like site renders the chicken glutamine-synthetase gene hormonally indudble in transfected retina. ]. Biol. Chem., 266, 24332-8. 

---