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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Yang, Y. Inouye, M. |
| Description | Author Affiliation: Yang Y ( Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Rutgers-Robert Wood Johnson Medical School, Piscataway 08854.); |
| Abstract | Taz1 is a hybrid signal-transducing membrane receptor between Tar, an aspartate chemoreceptor, and EnvZ, an osmosensor of Escherichia coli that is able to induce ompC expression by phosphorylating OmpR (a transcriptional activator) in response to aspartate. When the Taz1 His-277, the proposed autophosphorylation site in the cytoplasmic EnvZ domain, was replaced with a valine residue, the mutant Taz1 was unable to induce ompC expression. Similarly, when approximately two-thirds of the EnvZ domain was deleted, Taz1 was nonfunctional. However, when these two defective Taz1 proteins were coexpressed in a cell, ompC was constitutively expressed. Coinciding with this result, two mutant Taz1 molecules were able to intermolecularly complement each other to restore the OmpR kinase activity but not phosphatase activity in vitro. The identical result was also obtained with EnvZ. The present results suggest that the autophosphorylation of Taz1 and EnvZ is an intermolecular phosphorylation reaction, requiring formation of a dimer (or oligomer), and that ligand-dependent ompC expression requires not only kinase but also phosphatase activity. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 24 |
| Volume Number | 88 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1991-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacterial Outer Membrane Proteins Genetics Escherichia Coli Proteins Escherichia Coli Membrane Proteins Multienzyme Complexes Phosphoprotein Phosphatases Protein Kinases Signal Transduction Amino Acid Sequence Metabolism Cell Membrane Chromosome Deletion Physiology Genetic Complementation Test Molecular Sequence Data Mutagenesis, Site-Directed Phosphorylation Plasmids Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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