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Solution structure of GSP13 from Bacillus subtilis exhibits an S1 domain related to cold shock proteins

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Abstract

GSP13 encoded by gene yugI is a σB-dependent general stress protein in Bacillus subtilis, which can be induced by heat shock, salt stress, ethanol stress, glucose starvation, oxidative stress and cold shock. Here we report the solution structure of GSP13 and it is the first structure of S1 domain containing protein in Bacillus subtilis. The structure of GSP13 mainly consists of a typical S1 domain along with a C-terminal 50-residue flexible tail, different from the other known S1 domain containing proteins. Comparison with other S1 domain structures reveals that GSP13 has a conserved RNA binding surface, and it may function similarly to cold shock proteins in response to cold stress.

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References

  • Antelmann H, Bernhardt J, Schmid R, Mach H, Völker U, Hecker M (1997) First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis. Electrophoresis 18:1451–1463

    Article  Google Scholar 

  • Bernhardt J, Völker U, Völker A, Antelmann H, Schmid R, Mach H, Hecker M (1997) Specific and general stress proteins in Bacillus subtilis—a two-deimensional protein electrophoresis study. Microbiology 143:999–1017

    Article  Google Scholar 

  • Bycroft M, Hubbard TJ, Proctor M, Freund SM, Murzin AG (1997) The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell 88:235–242

    Article  Google Scholar 

  • Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289–302

    Article  Google Scholar 

  • 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 6:277–293

    Article  Google Scholar 

  • Duggan BM, Legge GB, Dyson HJ, Wright PE (2001) SANE (Structure assisted NOE evaluation): an automated model-based approach for NOE assignment. J Biomol NMR 19:321–329

    Article  Google Scholar 

  • Haldenwang WG, Losick R (1980) Novel RNA polymerase sigma factor from Bacillus subtilis. Proc Natl Acad Sci USA 77:7000–7004

    Article  ADS  Google Scholar 

  • Hecker M, Pane-Farre J, Völker U (2007) SigB-dependent general stress response in Bacillus subtilis and related gram-positive bacteria. Annu Rev Microbiol 61:215–236

    Article  Google Scholar 

  • Herrmann T, Guntert P, Wüthrich K (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319:209–227

    Article  Google Scholar 

  • Johnson BA, Blevins RA (1994) NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4:603–614

    Article  Google Scholar 

  • Johnson SJ, Close D, Robinson H, Vallet-Gely I, Dove SL, Hill CP (2008) Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa. J Mol Biol 377:1460–1473

    Article  Google Scholar 

  • Kaan T, Homuth G, Mader U, Bandow J, Schweder T (2002) Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response. Microbiology 148:3441–3455

    Google Scholar 

  • Koradi R, Billeter M, Wüthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14(51–55):29–32

    Google Scholar 

  • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8:477–486

    Article  Google Scholar 

  • Maiti R, Van Domselaar GH, Zhang H, Wishart DS (2004) SuperPose: a simple server for sophisticated structural superposition. Nucleic Acids Res 32:W590–594

    Article  Google Scholar 

  • Nanamiya H, Akanuma G, Natori Y, Murayama R, Kosono S, Kudo T, Kobayashi K, Ogasawara N, Park SM, Ochi K, Kawamura F (2004) Zinc is a key factor in controlling alternation of two types of L31 protein in the Bacillus subtilis ribosome. Mol Microbiol 52:273–283

    Article  Google Scholar 

  • Pearlman DA, Case DA, Caldwell JW, Ross WS, Cheatham TE, Debolt S, Ferguson D, Seibel G, Kollman P (1995) Amber, a package of computer-programs for applying molecular mechanics, normal-mode analysis, molecular-dynamics and free-energy calculations to simulate the structural and energetic properties of molecules. Comp Phys Commun 91:1–41

    Article  MATH  ADS  Google Scholar 

  • Weber MH, Beckering CL, Marahiel MA (2001) Complementation of cold shock proteins by translation initiation factor IF1 in vivo. J Bacteriol 183:7381–7386

    Article  Google Scholar 

  • Xia B, Ke H, Inouye M (2001) Acquirement of cold sensitivity by quadruple deletion of the cspA family and its suppression by PNPase S1 domain in Escherichia coli. Mol Microbiol 40:179–188

    Article  Google Scholar 

  • Yu W, Yu B, Hu J, Xia W, Jin C, Xia B (2008) 1H, 13C, and 15N resonance assignments of a general stress protein GSP13 from Bacillus subtilis. Biomolecular NMR Assignments 2:163–165

    Article  Google Scholar 

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Acknowledgments

All NMR experiments were carried out at the Beijing NMR Center. We thank Dr. Xiao-Dong Su for providing us the genome library of Bacillus subtilis. This research was supported by Grant 30125009 to BX from the National Science Foundation of China and grant 2006AA02A323 to CJ from the 863 Program.

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Authors and Affiliations

  1. Beijing Nuclear Magnetic Resonance Center, College of Life Sciences, Peking University, Beijing, 100871, China

    Wenyu Yu, Jicheng Hu, Bingke Yu, Wei Xia, Changwen Jin & Bin Xia

  2. College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China

    Changwen Jin & Bin Xia

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  1. Wenyu Yu
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  2. Jicheng Hu
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  3. Bingke Yu
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  4. Wei Xia
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  5. Changwen Jin
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  6. Bin Xia
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Correspondence to Bin Xia.

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Yu, W., Hu, J., Yu, B. et al. Solution structure of GSP13 from Bacillus subtilis exhibits an S1 domain related to cold shock proteins. J Biomol NMR 43, 255–259 (2009). https://doi.org/10.1007/s10858-009-9298-y

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  • DOI: https://doi.org/10.1007/s10858-009-9298-y

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