Solution structures of RseA and its complex with RseB.
The bacterial envelope stress response, which is responsible for sensing stress signals in the envelope and for turning on the sigma(E)-dependent transcription, is modulated by the binding of RseB to RseA. In this study, the solution structures of RseA and its complex with RseB were analyzed using circular dichroism and small-angle X-ray scattering. The periplasmic domain of RseA is unstructured and flexible when it is not bound to RseB. However, upon the formation of the stable complex with RseB, RseA induces conformational changes in RseB and, at the same time, RseA becomes more structured. Furthermore, it appears that some other undefined region of RseA, as well as the previously identified minimum region (amino acid 169-186), is also involved in RseB binding. It is thought that these conformational changes are relevant to the proteolytic cleavage of RseA and the modulation of envelope stress response.
Jin
Kyeong Sik
KS
Department of Chemistry, National Research Laboratory for Polymer Synthesis and Physics, Pohang Accelerator Laboratory, Center for Integrated Molecular Systems, Polymer Research Institute, Pohang 790-784, Republic of Korea.
Kim
Dong Young
DY
Rho
Yecheol
Y
Le
Van Binh
VB
Kwon
Eunju
E
Kim
Kyeong Kyu
KK
Ree
Moonhor
M
D002942:Circular Dichroism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D006868:Hydrolysis; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D012542:Scattering, Radiation; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism
D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C433802:RseA protein, E coli; C494790:RseB protein, E coli; D014157:Transcription Factors