Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Phototropin-related NPL1 controls chloroplast relocation induced by blue light

Nature volume 410, pages 952–954 (2001)Cite this article

Abstract

In photosynthetic cells, chloroplasts migrate towards illuminated sites to optimize photosynthesis and move away from excessively illuminated areas to protect the photosynthetic machinery1. Although this movement of chloroplasts in response to light has been known for over a century, the photoreceptor mediating this process has not been identified. The Arabidopsis gene NPL1 (ref. 2) is a paralogue of the NPH1 gene, which encodes phototropin, a photoreceptor for phototropic bending3. Here we show that NPL1 is required for chloroplast relocation induced by blue light. A loss-of-function npl1 mutant showed no chloroplast avoidance response in strong blue light, whereas the accumulation of chloroplasts in weak light was normal. These results indicate that NPL1 may function as a photoreceptor mediating chloroplast relocation.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Tissue expression and light inducibility of NPL1 mRNA.
Figure 2: Chloroplast movement in response to continuous blue light.

Similar content being viewed by others

References

  1. Zurzycki, J. in Blue-light Syndrome (ed. Senger, H.) 50–68 (Springer, Berlin, 1980).

    Book  Google Scholar 

  2. Jarillo, J. A., Ahmad, M. & Cashmore, A. R. NPL1 (Accession number AF053941): a second member of the NPH serine/threonine kinase family of Arabidopsis. Plant Physiol. 117, 719 (1998).

    Google Scholar 

  3. Huala, E. et al. Arabidopsis NPH1: a protein kinase with a putative redox-sensing domain. Science 278, 2120–2123 (1997).

    Article  ADS  CAS  Google Scholar 

  4. Wada, M., Grolig, F. & Haupt, W. Light-oriented chloroplast positioning. Contribution to progress in photobiology. J. Photochem. Photobiol. 17, 3–25 (1993).

    Article  CAS  Google Scholar 

  5. Kadota, A., Sato, Y. & Wada, M. Intracellular chloroplast photorelocation in the moss Physcomitrella patents is mediated by phytochrome as well as a blue-light receptor. Planta 210, 932–937 (2000).

    Article  CAS  Google Scholar 

  6. Briggs, W. R. & Huala, E. Blue-light photoreceptors in higher plants. Annu. Rev. Cell Dev. Biol. 15, 33–62 (1999).

    Article  CAS  Google Scholar 

  7. Zacherl, M., Huala, E., Rudiger, W., Briggs, W. R. & Salomon, M. Isolation and characterization of cDNAs from oat encoding a serine/threonine kinase: an early component in signal transduction for phototropism. Plant Physiol. 116, 869 (1998).

    Google Scholar 

  8. Kanegae, H. et al. Rice NPH1 homologues, OsNPH1a and OsNPH1b, are differently photoregulated. Plant Cell. Physiol. 41, 415–423 (2000).

    Article  CAS  Google Scholar 

  9. Nozue, K., Christie, J. M., Kiyosue, T., Briggs, W. R. & Wada, M. Isolation and characterization of a fern phototropin (Accession number AB037188), a putative blue-light photoreceptor for phototropism. Plant Physiol. 122, 1457 (2000).

    Article  Google Scholar 

  10. Salomon, M., Christie, J. M., Knieb, E., Lempert, U. & Briggs, W. R. Photochemical and mutational analysis of the FMN-binding domains of the plant blue light photoreceptor, phototropin. Biochemistry 39, 9401–9410 (2000).

    Article  CAS  Google Scholar 

  11. Hanks, S. K., Quinn, A. M. & Hunter, T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241, 42–52 (1988).

    Article  ADS  CAS  Google Scholar 

  12. Liscum, E. & Briggs, W. R. Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli. Plant Cell 7, 473–485 (1995).

    CAS  PubMed  PubMed Central  Google Scholar 

  13. Lin, C. Photoreceptors and regulation of flowering time. Plant Physiol. 123, 39–50 (2000).

    Article  CAS  Google Scholar 

  14. Kagawa, T. & Wada, M. Blue light-induced chloroplast relocation in Arabidopsis thaliana as analyzed by microbeam irradiation. Plant Cell Physiol. 41, 84–93 (2000).

    Article  CAS  Google Scholar 

  15. Trojan, A. & Gabrys, H. Chloroplast distribution in Arabidopsis thaliana (L.) depends on light conditions during growth. Plant Physiol. 111, 419–425 (1996).

    Article  CAS  Google Scholar 

  16. Tlalka, M. & Gabrys, H. Influence of calcium on blue-light-induced chloroplast movement in Lemna trisulca. Planta 189, 491–498 (1993).

    Article  CAS  Google Scholar 

  17. Malec, P. Kinetic modelling of chloroplast phototranslocations in Lemna trisulca L: two rate-limiting components? J. Theor. Biol. 169, 189–195 (1994).

    Article  Google Scholar 

  18. Ahmad, M. & Cashmore, A. R. HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor. Nature 366, 162–166 (1993).

    Article  ADS  CAS  Google Scholar 

  19. Leutwiler, L. S., Meyerowitz, E. & Tobin, E. M. Structure and expression of three light-harvesting chlorophyll a/b binding protein genes of Arabidopsis thaliana. Nucleic Acids Res. 14, 4051–4064 (1986).

    Article  CAS  Google Scholar 

  20. Walczak, T. & Gabrys, H. New type of photometer for measurements of transmission changes corresponding to chloroplast movements in leaves. Photosynthetica 14, 65–72 (1980).

    Google Scholar 

Download references

Acknowledgements

This work was supported by grants to A.R.C. from NIH and DOE, and a NATO fellowship awarded to J.C. We thank N. Bonini and S. Poethig for comments on the manuscript.

Author information

Author notes

  1. Jose M. Alonso & Joseph R. Ecker

    Present address: Plant Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, California, 92037, USA

Authors and Affiliations

  1. Department of Biology, Plant Science Institute, University of Pennsylvania, Philadelphia, 19104-6018, Pennsylvania, USA

    Jose A. Jarillo, Juan Capel, Jose M. Alonso, Joseph R. Ecker & Anthony R. Cashmore

  2. Institute of Molecular Biology, Jagiellonian University, Krakow, 31-120, Poland

    Halina Gabrys

  3. Departamento de Biología Aplicada, Universidad de Almería, Almeria, 04120, Spain

    Juan Capel

Authors
  1. Jose A. Jarillo
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Halina Gabrys
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Juan Capel
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Jose M. Alonso
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Joseph R. Ecker
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Anthony R. Cashmore
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Anthony R. Cashmore.

Supplementary information

Figure 1.

Comparisons of conserved domains in NPL1 and other members of the NPH1 protein family. Sequence alignments of AtNPL1 (Accession number, AF053941), and AtNPH1 (Accession number, AF030864) from Arabidopsis thaliana, OsNPH1a (Accession number, AB018444.1), and OsNPH1b (Accession number, AB018443.1) from Oryza sativa, AsNPH1-1 (Accession number, AF033096), and AsNPH1-2 (Accession number, AF033097) from Avena sativa L., ZmNPH1 (Accession number, AF033263) from Zea mays, and AcNPH1-2 (Accession number, AB037188) from Adiantum capillus-veneris. The LOV domains are highlighted by a line below the sequence. A double line indicates the serine-threonine kinase domain. Asterisks represent the conserved cysteine residues involved in the photochemical reactions of the NPH1 LOV domains. (GIF 285 KB)

Figure 2.

Isolation and phenotypic characterization of npl1 mutant. a. NPL1 gene structure and T-DNA insertion mutant. The NPL1 gene that maps to the bottom of chromosome V, bears a coding region of 22 exons (represented by filled boxes) extending for 5.4 Kb. The npl1-1 mutant was identified by PCR-screening of 30,000 T-DNA insertion lines (Alonso and Ecker, unpublished), using oligonucleotides specific for the NPL1 gene and the T-DNA. By DNA sequencing of the amplified products, it was demonstrated that the insertion disrupted the NPL1 gene in the second intron (the site of the T-DNA insertion in the npl1 mutant is indicated). b. Northern blot hybridization with an NPL1 probe against RNA prepared from leaves of wild type (Columbia) and npl1mutant plants. The band in the wild type lane corresponded to a size of approximately 3 kb. No hybridization signal was detected for the mutant. (GIF 12 KB)

Rights and permissions

Reprints and permissions

About this article

Cite this article

Jarillo, J., Gabrys, H., Capel, J. et al. Phototropin-related NPL1 controls chloroplast relocation induced by blue light. Nature 410, 952–954 (2001). https://doi.org/10.1038/35073622

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/35073622

This article is cited by

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing