Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism.

@article{citeulike:2919593, abstract = {We demonstrate by using purified bacterial components that the protein kinases that regulate chemotaxis and transcription of nitrogen-regulated genes, CheA and NRII, respectively, have cross-specificities: CheA can phosphorylate the Ntr transcription factor NRI and thereby activate transcription from the nitrogen-regulated glnA promoter, and NRII can phosphorylate CheY. In addition, we find that a high intracellular concentration of a highly active mutant form of NRII can suppress the smooth-swimming phenotype of a cheA mutant. These results argue strongly that sensory transduction in the Ntr and Che systems involves a common protein phosphotransfer mechanism.}, address = {Department of Molecular Biology, Princeton University, NJ 08540.}, author = {Ninfa, A. J. and Ninfa, E. G. and Lupas, A. N. and Stock, A. and Magasanik, B. and Stock, J. }, citeulike-article-id = {2919593}, issn = {0027-8424}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {bacteria, chemotaxis, crosstalk, phosphorylation, transcriptional\_regulation, two-component\_system}, month = {August}, number = {15}, pages = {5492--5496}, posted-at = {2008-06-23 20:02:54}, priority = {0}, title = {Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/3041412}, volume = {85}, year = {1988} }

TY - JOUR ID - citeulike:2919593 L3 - citeulike-article-id:2919593 TI - Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism. JF - Proceedings of the National Academy of Sciences of the United States of America VL - 85 IS - 15 SP - 5492 EP - 5496 AD - Department of Molecular Biology, Princeton University, NJ 08540. SN - 0027-8424 N2 - We demonstrate by using purified bacterial components that the protein kinases that regulate chemotaxis and transcription of nitrogen-regulated genes, CheA and NRII, respectively, have cross-specificities: CheA can phosphorylate the Ntr transcription factor NRI and thereby activate transcription from the nitrogen-regulated glnA promoter, and NRII can phosphorylate CheY. In addition, we find that a high intracellular concentration of a highly active mutant form of NRII can suppress the smooth-swimming phenotype of a cheA mutant. These results argue strongly that sensory transduction in the Ntr and Che systems involves a common protein phosphotransfer mechanism. KW - bacteria KW - chemotaxis KW - crosstalk KW - phosphorylation KW - transcriptional_regulation KW - two-component_system AU - Ninfa, AJ AU - Ninfa, EG AU - Lupas, AN AU - Stock, A AU - Magasanik, B AU - Stock, J PY - 1988/08// UR - http://view.ncbi.nlm.nih.gov/pubmed/3041412 ER -