Abstract
Cyclophilins are omnipresent proteins found in eukaryotes and prokaryotes, with presence in cytoplasm as well as in nucleus. Primary role of Cyclophilins is of peptidyl-prolyl cis–trans isomerase, a molecular chaperon action. Here, we report sequence-specific 1H, 13C and 15N resonance assignments for a Cyclophilin A like protein from Piriformospora indica. This protein is up-regulated during salt stress conditions.
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References
Bhavesh NS, Panchal SC, Hosur RV (2001) An efficient high-throughput resonance assignment procedure for structural genomics and protein folding research by NMR. Biochemistry 40:14727–14735
Das A, Kamal S, Shakil NA, Sherameti I, Oelmüller R, Dua M, Tuteja N, Johri AK, Varma A (2012) The root endophyte fungus Piriformospora indica leads to early flowering, higher biomass and altered secondary metabolites of the medicinal plant, Coleus forskohlii. Plant Signal Behav 7:103–112
Davis TL, Walker JR, Campagna-Slater V, Finerty PJ Jr, Paramanathan R, Bernstein G, MacKenzie F, Tempel W, Ouyang H, Lee WH, Eisenmesser EZ, Dhe-Paganon S (2010) Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PLoS Biol 8:e1000439
Keller R (2004) The computer aided resonance assignment tutorial, 1st edn. CANTINA Verlag. ISBN 3-85600-112-3
Tuteja N (2007) Mechanisms of high salinity tolerance in plants. Meth Enzymol 428:419–438
Verma S, Varma A, Rexer KH, Hassel A, Kost G, Sarbhoy A, Bisen P, Bütehorn B, Franken P (1998) Piriformospora indica, gen. et sp. nov., a new root-colonizing fungus. Mycologia 90:896–903
Waller F, Achatz B, Baltruschat H, Fodor J, Becker K, Fischer M, Heier T, Hückelhoven R, Neumann C, Wettstein DV, Franken P, Kogel K (2005) The endophytic fungus Piriformospora indica reprograms barley to salt-stress tolerance, disease resistance, and higher yield. PNAS 102:13386–13391
Wang P, Heitman J (2005) The cyclophilins. Genome Biol 6:226
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 4:171–180
Xiong L, Schumaker KS, Zhu J (2002) Cell signaling during cold, drought, and salt stress. Plant Cell 14:165–183
Acknowledgments
This study is supported by grants to NT and NSB from Department of Science and Technology (DST), Government of India and ICGEB core funds. We thank Department of Biotechnology (DBT), Government of India for providing financial support for the 500 MHz and 700 MHz NMR spectrometers at the ICGEB, New Delhi and NII, New Delhi. We thank Prof. Virander S. Chauhan for his interest and support in establishing the NMR facility. DKT is a recipient of Department of Biotechnology (DBT) junior research fellowship. HB is a recipient of Council for Scientific and Industrial Research (CSIR) senior research fellowship.
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Dipesh Kumar Trivedi and Harshesh Bhatt contributed equally to this work.
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Trivedi, D.K., Bhatt, H., Johri, A. et al. Sequence-specific 1H, 13C and 15N NMR assignments of Cyclophilin A like protein from Piriformospora indica involved in salt stress tolerance. Biomol NMR Assign 7, 175–178 (2013). https://doi.org/10.1007/s12104-012-9404-z
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DOI: https://doi.org/10.1007/s12104-012-9404-z