Backbone and side chain NMR assignment, along with the secondary structure prediction of RRM2 domain of La protein from a lower eukaryote exhibiting identical structural organization with its human homolog

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• 作者：Aikaterini I. Argyriou (1)
  Christos T. Chasapis (1)
  Maria Apostolidi (3)
  Parthena Konstantinidou (3)
  Constantinos Stathopoulos (3)
  Detlef Bentrop (2)
  Georgios A. Spyroulias (1)
  
  1. Department of Pharmacy ; University of Patras ; 26504 ; Patras ; Greece
  3. Department of Biochemistry ; School of Medicine ; University of Patras ; 26504 ; Patras ; Greece
  2. Institute of Physiology II ; University of Freiburg ; 79104 ; Freiburg ; Germany
  
• 关键词：La protein ; RNA polymerase III ; RNA binding ; Recombinant protein expression ; NMR spectroscopy
• 刊名：Biomolecular NMR Assignments
• 出版年：2015
• 出版时间：April 2015
• 年：2015
• 卷：9
• 期：1
• 页码：219-222
• 全文大小：389 KB
• 参考文献：1. Apostolidi, M, Vourtsis, DJ, Chasapis, CT, Stathopoulos, C, Bentrop, D, Spyroulias, GA (2014) 1H, 15N, 13C assignment and secondary structure determination of two domains of La protein from D. discoideum. Biomol NMR Assign 8: pp. 47-51 CrossRef
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  3. Bayfield, MA, Yang, R, Maraia, RJ (2010) Conserved and divergent features of the structure and function of La and La-related proteins (LARPs). Biochim Biophys Acta 1799: pp. 365-378 CrossRef
  4. Bousquet-Antonelli, C, Deragon, JM (2009) A comprehensive analysis of the La-motif protein superfamily. RNA 15: pp. 750-764 CrossRef
  5. Jacks, A, Kelly, G, Curry, S, Conte, MR (2002) Resonance assignment and secondary structure determination of a C-terminal fragment of the lupus autoantigen (La) protein containing a putative RNA recognition motif (RRM). J Biomol NMR 22: pp. 387-388 CrossRef
  6. Jacks, A, Babon, J, Kelly, G, Manolaridis, I, Cary, PD, Curry, S, Conte, MR (2003) Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element. Structure 7: pp. 833-843 CrossRef
  7. Keller, R (2004) The computer aided resonance assignment tutorial CH-6410. Cantina Verlag, Goldau
  8. Liang, C, Xiong, K, Szulwach, KE, Zhang, Y, Wang, Z, Peng, J, Fu, M, Jin, P, Suzuki, HI, Liu, Q (2013) Sjogren syndrome antigen B (SSB)/La promotes global microRNA expression by binding microRNA precursors through stem-loop recognition. J Biol Chem 288: pp. 723-736 CrossRef
  9. Maraia, RJ, Bayfield, MA (2006) The La protein-RNA complex surfaces. Mol Cell 21: pp. 149-152 CrossRef
  10. Maraia, RJ, Intine, RVA (2001) Recognition of nascent RNA by the human La antigen: conserved and divergent features of structure and function. Mol Cell Biol 21: pp. 367-379 CrossRef
  11. Schubert, M, Labudde, D, Oschkinat, H, Schmieder, P (2002) A software tool for the prediction of Xaa-Pro peptide bond conformations in proteins based on 13C chemical shift statistics. J Biomol NMR 24: pp. 149-154 CrossRef
  12. Shen, Y, Delaglio, F, Cornilescu, G, Bax, A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44: pp. 213-223 CrossRef
  13. Wolin, SL, Cedervall, T (2002) The La protein. Annu Rev Biochem 71: pp. 375-403 CrossRef
  
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X

文摘

The La protein (Lupus antigen), a key mediator during biogenesis of RNA polymerase III transcripts, contains a characteristic La motif and one or two RNA recognition motif (RRM) domains, depending on the organism of origin. The RRM1 domain is conserved in higher eukaryotes and located in the N-terminal region, whereas the C-terminal RRM2 domain is absent in most lower eukaryotes and its specific role remains, so far, uncharacterized. Here, we present the backbone and side-chain assignment of the 1H, 13C and 15N resonances of RRM2 of La protein from Dictyostelium discoideum. Interestingly, the La protein in this lower eukaryote, exhibits high homology to its human counterpart. Moreover, it contains two RRM domains, instead of one, raising questions on its evolutionary origin and the putative role of RRM2 in vivo. We also provide its secondary structure as predicted by the TALOS+ online tool.