RssB-mediated σS Activation is Regulated by a Two-Tier Mechanism via Phosphorylation and Adaptor Protein – IraD |
| |
| Institution: | 1. BioBank, The First Affiliated Hospital of Xi''an Jiaotong University, Shaanxi 710061, China;2. Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, SW7 2AZ London, United Kingdom;3. Instrument Analysis Center of Xi''an Jiaotong University, Xi''an, Shaanxi 710049, China;4. School of Pharmacy, Xi''an Jiaotong University, Xi''an 710061, China;5. National Facility for Protein Science, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, China;1. SCITEC-CNR, via Mario Bianco 9, 20131 Milan, Italy;2. Department of Chemistry, University of Pavia, via Taramelli 12, 27100 Pavia, Italy;1. Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, United States;2. Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX, United States;3. Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, United States;1. Institute of Structural Biology, University of Bonn, 53127 Bonn, Germany;2. Physical and Synthetic Biology, Faculty of Biology, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany;3. Molecular Microscopy Research Group, Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands;4. Department of Biology (Area 10), University of York, York YO10 5YW, UK;1. Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, 4202 E. Fowler Ave., Tampa, FL 33620, USA;2. Physics and Materials Science Research Unit, University of Luxembourg, L-1511 Luxembourg, Luxembourg;3. Department of Physics, University of South Florida, 4202 E. Fowler Ave., Tampa, FL 33620, USA;1. Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA;2. The Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA;3. Department of Biophysics, Medical College of Wisconsin, Milwaukee, WI 53226, USA;4. The Biophysics Collaborative Access Team (BioCAT), Department of Biological Chemical and Physical Sciences, Illinois Institute of Technology, Chicago, IL 60616, USA;5. University of California Los Angeles, Los Angeles, CA 90095, USA;6. Department of Biochemistry and the Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN 37232, USA;1. Department of Molecular Genetics and Infection Biology, Interfaculty Institute for Genetics and Functional Genomics, Center for Functional Genomics of Microbes, University of Greifswald, D-17487 Greifswald, Germany;2. Department of Crystallography and Structural Biology, Institute of Physical Chemistry “Rocasolano”, CSIC, 28006 Madrid, Spain;3. Cellular Metabolism/Metabolomics, Institute of Biochemistry, University of Greifswald, D-17487 Greifswald, Germany;4. Present Address: Institut für Klinische Chemie und Laboratoriumsmedizin, Universitätsmedizin Greifswald, Germany;5. Present Address: Institute for Microbiology, University of Veterinary Medicine Hannover, Hannover, Germany;6. Present Address: Biochemie der Pflanzen, Heinrich-Heine-Universität Düsseldorf, Germany;7. Present Address: Structural Molecular Biology Group, Novo Nordisk Foundation Centre for Protein Research, Faculty of Health and Medical Sciences University of Copenhagen, Blegdamsvej 3-B, Copenhagen, 2200, Denmark |
| |
| Abstract: | Regulation of bacterial stress responding σS is a sophisticated process and mediated by multiple interacting partners. Controlled proteolysis of σS is regulated by RssB which maintains minimal level of σS during exponential growth but then elevates σS level while facing stresses. Bacteria developed different strategies to regulate activity of RssB, including phosphorylation of itself and production of anti-adaptors. However, the function of phosphorylation is controversial and the mechanism of anti-adaptors preventing RssB-σS interaction remains elusive. Here, we demonstrated the impact of phosphorylation on the activity of RssB and built the RssB-σS complex model. Importantly, we showed that the phosphorylation site - D58 is at the interface of RssB-σS complex. Hence, mutation or phosphorylation of D58 would weaken the interaction of RssB with σS. We found that the anti-adaptor protein IraD has higher affinity than σS to RssB and its binding interface on RssB overlaps with that for σS. And IraD-RssB complex is preferred over RssB-σS in solution, regardless of the phosphorylation state of RssB. Our study suggests that RssB possesses a two-tier mechanism for regulating σS. First, phosphorylation of RssB provides a moderate and reversible tempering of its activity, followed by a specific and robust inhibition via the anti-adaptor interaction. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
