Advertisement

1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli

  • Moye Jia
  • Yunfei HuEmail author
  • Changwen JinEmail author
Article
  • 35 Downloads

Abstract

The periplasmic chaperone SurA in Gram-negative bacteria plays a central role in the biogenesis of integral outer membrane proteins and is critical to the maintenance of bacterial membrane integrity. SurA contains a core chaperone module comprising the N- and C-terminal domains, along with two peptidyl-prolyl isomerase (PPIase) domains. The chaperone activity of SurA has been demonstrated to rely on the core module, whereas recent works suggested that the PPIase domains may regulate the chaperone activity through large conformational rearrangements. Herein, we report the resonance assignments of 1H, 13C and 15N atoms of the second PPIase domain of Escherichia coli SurA, which provide valuable information for further studies of the structure, dynamics and interactions of this chaperone using NMR techniques.

Keywords

Chaperone SurA PPIase domain 

Notes

Acknowledgements

All NMR experiments were carried out at the Beijing NMR Center. We thank Dr. Hongwei Li at Beijing NMR Center for assistance in NMR data collection. This work was supported by Grant 31370718 from the National Natural Science Foundation of China to Y. H. and Grant 2016YFA0501201 from the National Key R&D Program of China to C. J.

References

  1. Behrens S, Maier R, de Cock H, Schmid FX, Gross CA (2001) The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J 20:285–294CrossRefGoogle Scholar
  2. Bitto E, McKay DB (2002) Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure 10:1489–1498CrossRefGoogle Scholar
  3. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293CrossRefGoogle Scholar
  4. Johnson BA, Blevins RA (1994) NMR View: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4:603–614CrossRefGoogle Scholar
  5. Lazar SW, Kolter R (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178:1770–1773CrossRefGoogle Scholar
  6. Marley J, Lu M, Bracken C (2001) A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 20:71–75CrossRefGoogle Scholar
  7. Nikaido H (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67:593–656CrossRefGoogle Scholar
  8. Rouviere PE, Gross CA (1996) SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev 10:3170–3182CrossRefGoogle Scholar
  9. Ruiz N, Kahne D, Silhavy TJ (2006) Advances in understanding bacterial outer-membrane biogenesis. Nat Rev Microbiol 4:57–66CrossRefGoogle Scholar
  10. Sklar JG, Wu T, Kahne D, Silhavy TJ (2007) Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev 21:2473–2484CrossRefGoogle Scholar
  11. Soltes GR, Schwalm J, Ricci DP, Silhavy TJ (2016) The activity of Escherichia coli chaperone SurA is regulated by conformational changes involving a parvulin domain. J Bacteriol 198:921–929CrossRefGoogle Scholar
  12. Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180CrossRefGoogle Scholar
  13. Wulfing C, Pluckthun A (1994) Protein folding in the periplasm of Escherichia coli. Mol Microbiol 12:685–692CrossRefGoogle Scholar
  14. Xu X, Wang S, Hu YX, McKay DB (2007) The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues. J Mol Biol 373:367–381CrossRefGoogle Scholar

Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.College of Life SciencesPeking UniversityBeijingChina
  2. 2.College of Chemistry and Molecular EngineeringPeking UniversityBeijingChina
  3. 3.Beijing Nuclear Magnetic Resonance CenterPeking UniversityBeijingChina
  4. 4.Beijing National Laboratory for Molecular SciencesPeking UniversityBeijingChina
  5. 5.Medical College of Soochow UniversitySuzhouChina

Personalised recommendations