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1H, 13C, and 15N chemical shift assignments of cyanobacteriochrome NpR6012g4 in the green-absorbing photoproduct state

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Abstract

Cyanobacteriochromes (CBCRs) are cyanobacterial photosensory proteins with a tetrapyrrole (bilin) chromophore that belong to the phytochrome superfamily. Like phytochromes, CBCRs photoconvert between two photostates with distinct spectral properties. NpR6012g4 from Nostoc punctiforme is a model system for widespread CBCRs with conserved red/green photocycles. Atomic-level structural information for the photoproduct state in this subfamily is not known. Here, we report NMR backbone chemical shift assignments of the light-activated state of NpR6012g4 (BMRB no. 26577) as a first step toward determining its atomic resolution structure.

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References

  • Auldridge ME, Forest KT (2011) Bacterial phytochromes: more than meets the light. Crit Rev Biochem Mol Biol 46:67–88

    Article  Google Scholar 

  • Campbell EL, Hagen KD, Chen R, Risser DD, Ferreira DP, Meeks JC (2015) Genetic analysis reveals the identity of the photoreceptor for phototaxis in hormogonium filaments of Nostoc punctiforme. J Bacteriol 197:782–791

    Article  Google Scholar 

  • Enomoto G, Ni-Ni W, Narikawa R, Ikeuchi M (2015) Three cyanobacteriochromes work together to form a light color-sensitive input system for c-di-GMP signaling of cell aggregation. Proc Natl Acad Sci USA 112:8082–8087

    Article  ADS  Google Scholar 

  • Gambetta GA, Lagarias JC (2001) Genetic engineering of phytochrome biosynthesis in bacteria. Proc Natl Acad Sci USA 98:10566–10571

    Article  ADS  Google Scholar 

  • Ikeuchi M, Ishizuka T (2008) Cyanobacteriochromes: a new superfamily of tetrapyrrole-binding photoreceptors in cyanobacteria. Photochem Photobiol Sci 7:1159–1167

    Article  Google Scholar 

  • Kim PW, Freer LH, Rockwell NC, Martin SS, Lagarias JC, Larsen DS (2012) Femtosecond photodynamics of the red/green cyanobacteriochrome NpR6012g4 from Nostoc punctiforme. 1. Forward dynamics. Biochemistry 51:608–618

    Article  Google Scholar 

  • Narikawa R, Ishizuka T, Muraki N, Shiba T, Kurisu G, Ikeuchi M (2013) Structures of cyanobacteriochromes from phototaxis regulators AnPixJ and TePixJ reveal general and specific photoconversion mechanism. Proc Natl Acad Sci USA 110:918–923

    Article  ADS  Google Scholar 

  • Rockwell NC, Martin SS, Lagarias JC (2012) Red/green cyanobacteriochromes: sensors of color and power. Biochemistry 51:9667–9677

    Article  Google Scholar 

  • Rockwell NC, Martin SS, Gulevich AG, Lagarias JC (2014) Conserved phenylalanine residues are required for blue-shifting of cyanobacteriochrome photoproducts. Biochemistry 53:3118–3130

    Article  Google Scholar 

  • Rockwell NC, Martin SS, Lim S, Lagarias JC, Ames JB (2015a) Characterization of red/green cyanobacteriochrome NpR6012g4 by solution nuclear magnetic resonance spectroscopy: a hydrophobic pocket for the C15-E, anti chromophore in the photoproduct. Biochemistry 54:3772–3783

    Article  Google Scholar 

  • Rockwell NC, Martin SS, Lim S, Lagarias JC, Ames JB (2015b) Characterization of red/green cyanobacteriochrome NpR6012g4 by solution nuclear magnetic resonance spectroscopy: a protonated bilin ring system in both photostates. Biochemistry 54:2581–2600

    Article  Google Scholar 

  • Velazquez F, Utesch T, Narikawa R, Ikeuchi M, Mroqinski MA, Gartner W, Hildebrandt P (2013) Photoconversion mechanism of the second GAF domain of cyanobacteriochrome AnPixJ and the cofactor structure of its green-absorbing state. Biochemistry 52:4871–4880

    Article  Google Scholar 

  • Wishart DS, Sykes BD, Richards FM (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647–1651

    Article  Google Scholar 

Download references

Acknowledgments

We thank Bennett Addison for technical support and help with NMR experiments. This work was supported by a grant from the Chemical Sciences, Geosciences, and Biosciences Division, Office of Basic Energy Sciences, Office of Science, United States Department of Energy (DOE DE-FG02-09ER16117 to J.C.L. and J.B.A.), with partial support for NMR time from NIH Grant RR11973 to the UC Davis NMR facility.

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Authors and Affiliations

  1. Department of Chemistry, University of California, Davis, CA, 95616, USA

    Sunghyuk Lim, Qinhong Yu & James B. Ames

  2. Department of Molecular and Cellular Biology, University of California, Davis, CA, 95616, USA

    Nathan C. Rockwell, Shelley S. Martin & J. Clark Lagarias

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  1. Sunghyuk Lim
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  2. Qinhong Yu
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  3. Nathan C. Rockwell
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  4. Shelley S. Martin
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  5. J. Clark Lagarias
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  6. James B. Ames
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Correspondence to James B. Ames.

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Lim, S., Yu, Q., Rockwell, N.C. et al. 1H, 13C, and 15N chemical shift assignments of cyanobacteriochrome NpR6012g4 in the green-absorbing photoproduct state. Biomol NMR Assign 10, 157–161 (2016). https://doi.org/10.1007/s12104-015-9657-4

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  • DOI: https://doi.org/10.1007/s12104-015-9657-4

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