Biomolecular NMR Assignments

, Volume 11, Issue 2, pp 269–273 | Cite as

Backbone and side-chain 1H, 15N and 13C resonance assignments of two Sac10b family members Mvo10b and Mth10bTQQA from archaea

  • Jinsong Xuan
  • Hongwei Yao
  • Yingang FengEmail author
  • Jinfeng WangEmail author


The Sac10b family proteins, also named as Alba, are small, basic, nucleic acid-binding proteins widely distributed in archaea. They possess divergent physiological functions such as binding to both DNA and RNA with a high affinity and involving in genomic DNA compaction, RNA transactions and transcriptional regulations. The structures of many Sac10b family proteins from hyperthermophilic archaea have been reported, while those from thermophilic and mesophilic archaea are largely unknown. As was pointed out, the homologous members from thermophilic and mesophilic archaea may have functions different from the hyperthermophilic members. Therefore, comparison of these homologous members can provide biophysical and structural insight into the functional diversity and thermal adaptation mechanism. The present work mainly focused on the NMR study of two Sac10b family members, Mvo10b and Mth10b, from the mesophilic and thermophilic archaea, respectively. To overcome the difficulties caused by the oligomerization and conformation heterogeneity of Mth10b, a M13T/L17Q/I20Q/P56A mutant Mth10b (Mth10bTQQA) was constructed and used together with Mvo10b for multi-dimensional NMR experiments. The resonance assignments of Mvo10b and Mth10bTQQA are reported for further structural determination which is a basis for understanding the functional diversity and their thermal adaption mechanisms.


Sac10b family Mesophilic Thermal adaptation mechanism NMR assignments Archaea 



We thank Prof. Li Huang, Institute of Microbiology, Chinese Academy of Sciences, for kindly providing the genes of mvo10b and mth10b. This work was supported by the National Natural Science Foundation of China to J. Xuan (31300635) Y. Feng (31670735) and J. Wang (30770434).


  1. Campos EI, Reinberg D (2009) Histones: annotating chromatin. Annu Rev Genet 43:559–599. doi: 10.1146/annurev.genet.032608.103928 CrossRefGoogle Scholar
  2. Crnigoj M, Podlesek Z, Zorko M, Jerala R, Anderluh G, Ulrih NP (2013) Interactions of archaeal chromatin proteins Alba1 and Alba2 with nucleic acids. PLoS ONE 8(2):e58237. doi: 10.1371/journal.pone.0058237 ADSCrossRefGoogle Scholar
  3. Cui Q, Tong Y, Xue H, Huang L, Feng Y, Wang J (2003) Two conformations of archaeal Ssh10b - the origin of its temperature-dependent interaction with DNA. J Biol Chem 278(51):51015–51022. doi: 10.1074/jbc.M308510200 CrossRefGoogle Scholar
  4. 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(3):277–293. doi: 10.1007/bf00197809 CrossRefGoogle Scholar
  5. Fang X, Cui Q, Tong Y, Feng Y, Shan L, Huang L, Wang J (2008) A stabilizing alpha/beta-hydrophobic core greatly contributes to hyperthermostability of archaeal [P62A]Ssh10b. BioChemistry 47(43):11212–11221. doi: 10.1021/bi8007593 CrossRefGoogle Scholar
  6. Fang X, Feng Y, Wang J (2009) Favorable contribution of the C-terminal residue K97 to the stability of a hyperthermophilic archaeal [P62A]Ssh10b. Arch Biochem Biophys 481(1):52–58. doi: 10.1016/ CrossRefGoogle Scholar
  7. Ge M, Xia XY, Pan XM (2008) Salt bridges in the hyperthermophilic protein Ssh10b are resilient to temperature increases. J Biol Chem 283(46):31690–31696. doi: 10.1074/jbc.M805750200 CrossRefGoogle Scholar
  8. Goyal M, Banerjee C, Nag S, Bandyopadhyay U (2016) The Alba protein family: structure and function. Biochim Biophys Acta 1864(5):570–583. doi: 10.1016/j.bbapap.2016.02.015 CrossRefGoogle Scholar
  9. Guo L, Ding J, Guo R, Hou Y, Wang DC, Huang L (2014) Biochemical and structural insights into RNA binding by Ssh10b, a member of the highly conserved Sac10b protein family in Archaea. J Biol Chem 289(3):1478–1490. doi: 10.1074/jbc.M113.521351 CrossRefGoogle Scholar
  10. Jelinska C, Petrovic-Stojanovska B, Ingledew WJ, White MF (2010) Dimer–dimer stacking interactions are important for nucleic acid binding by the archaeal chromatin protein Alba. Biochem J 427(1):49–55. doi: 10.1042/BJ20091841 CrossRefGoogle Scholar
  11. Johnson BA, Blevins RA (1994) NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4(5):603–614. doi: 10.1007/BF00404272 CrossRefGoogle Scholar
  12. Laurens N, Driessen RP, Heller I, Vorselen D, Noom MC, Hol FJ, White MF, Dame RT, Wuite GJ (2012) Alba shapes the archaeal genome using a delicate balance of bridging and stiffening the DNA. Nat Commun 3:1328. doi: 10.1038/ncomms2330 ADSCrossRefGoogle Scholar
  13. Liu Y, Guo L, Guo R, Wong RL, Hernandez H, Hu J, Chu Y, Amster IJ, Whitman WB, Huang L (2009) The Sac10b homolog in Methanococcus maripaludis binds DNA at specific site. J Bacteriol 191(7):2315–2329. doi: 10.1128/JB.01534-08 CrossRefGoogle Scholar
  14. Luijsterburg MS, White MF, van Driel R, Dame RT (2008) The major architects of chromatin: architectural proteins in bacteria, archaea and eukaryotes. Crit Rev Biochem Mol Biol 43(6):393–418. doi: 10.1080/10409230802528488 CrossRefGoogle Scholar
  15. Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids. Pure Appl Chem 70(1):117–142. doi: 10.1351/pac199870010117 CrossRefGoogle Scholar
  16. Peeters E, Driessen RP, Werner F, Dame RT (2015) The interplay between nucleoid organization and transcription in archaeal genomes. Nat Rev Microbiol 13(6):333–341. doi: 10.1038/nrmicro3467 CrossRefGoogle Scholar
  17. Sattler M, Schleucher J, Griesinger C (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog Nucl Magn Reson Spectrosc 34:93–158. doi: 10.1016/S0079-6565(98)00025-9 CrossRefGoogle Scholar
  18. Shen Y, Bax A (2013) Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks. J Biomol NMR 56(3):227–241. doi: 10.1007/s10858-013-9741-y CrossRefGoogle Scholar
  19. Tanaka T, Padavattan S, Kumarevel T (2012) Crystal structure of archaeal chromatin protein Alba2-double-stranded DNA complex from Aeropyrum pernix K1. J Biol Chem 287(13):10394–10402. doi: 10.1074/jbc.M112.343210 CrossRefGoogle Scholar
  20. Wardleworth BN, Russell RJ, Bell SD, Taylor GL, White MF (2002) Structure of Alba: an archaeal chromatin protein modulated by acetylation. EMBO J 21(17):4654–4662. doi: 10.1093/emboj/cdf465 CrossRefGoogle Scholar
  21. Xuan J, Feng Y (2012) The archaeal Sac10b protein family: conserved proteins with divergent functions. Curr Protein Pept Sci 13(3):258–266. doi: 10.2174/138920312800785067 CrossRefGoogle Scholar
  22. Xuan J, Yao H, Feng Y, Wang J (2009) Cloning, expression and purification of DNA-binding protein Mvo10b from Methanococcus voltae. Protein Expr Purif 64(2):162–166. doi: 10.1016/j.pep.2008.11.003 CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2017

Authors and Affiliations

  1. 1.Department of Biological Science and Engineering, School of Chemical and Biological EngineeringUniversity of Science and Technology BeijingBeijingChina
  2. 2.High-Field Nuclear Magnetic Resonance Research CenterXiamen UniversityXiamenChina
  3. 3.Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of BioEnergy and Bioprocess TechnologyChinese Academy of SciencesQingdaoChina
  4. 4.National Laboratory of Biomacromolecules, Institute of BiophysicsChinese Academy of SciencesBeijingChina

Personalised recommendations