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A small heat-shock protein confers stress tolerance and stabilizes thylakoid membrane proteins in cyanobacteria under oxidative stress

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Abstract

Small heat-shock proteins are molecular chaperones that bind and prevent aggregation of nonnative proteins. They also associate with membranes. In this study, we show that the small heat-shock protein HspA plays a protective role under oxidative stress in the cyanobacterium Synechococcus elongatus strain ECT16-1, which constitutively expresses HspA. Compared with the reference strain ECT, ECT16-1 showed much better growth and viability in the presence of hydrogen peroxide. Under the peroxide stress, pigments in thylakoid membrane, chlorophyll, carotenoids, and phycocyanins, were continuously reduced in ECT, but in ECT16-1 they decreased only during the first 24 h of stress; thereafter no further reduction was observed. For comparison, we analyzed a wild type and an hspA deletion strain from Synechocystis sp. PCC 6803 and found that lack of hspA significantly affected the viability of the cell and the pigment content in the presence of methyl viologen, suggesting that HspA stabilizes membrane proteins such as the photosystems and phycobilisomes from oxidative damage. In vitro pull down assays showed a direct interaction of HspA with components of phycobilisomes. These results show that HspA and small heat-shock proteins in general play an important role in the acclimation to oxidative stress in cyanobacteria.

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Acknowledgment

K. S. was a recipient of a Japanese government scholarship for study in Japan.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Saitama University, Saitama, 338-8570, Japan

    Kollimalai Sakthivel, Tatsuro Watanabe & Hitoshi Nakamoto

Authors
  1. Kollimalai Sakthivel
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  2. Tatsuro Watanabe
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  3. Hitoshi Nakamoto
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Correspondence to Hitoshi Nakamoto.

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Communicated by Mary Allen.

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203_2009_457_MOESM1_ESM.tif

Supplementary Fig. 1. Cell growth (a), viability (b), and cellular absorption spectra of the Synechococcus ECT (c) and ECT16-1 (d) strains incubated in the presence of 0.8 mM hydrogen peroxide for 0, 24, 48, and 72 h. Diamonds and squares (a and b) represent ECT and ECT16-1, respectively. Cells were cultured at 30oC to approximately 0.3 apparent absorbance at 730 nm, and then (at 0 h) hydrogen peroxide was added to a final concentration of 0.8 mM (TIFF 8496 kb)

203_2009_457_MOESM2_ESM.tif

Supplementary Fig. 2. Cell growth (a), viability (b), and cellular absorption spectra of the Synechococcus ECT (c) and ECT16-1 (d) strains incubated in the presence of 0.9 mM hydrogen peroxide for 0, 24, 48, and 72 h. Diamonds and squares (a and b) represent ECT and ECT16-1, respectively. Cells were cultured at 30oC to approximately 0.3 apparent absorbance at 730 nm, and then (at 0 h) hydrogen peroxide was added to a final concentration of 0.9 mM (TIFF 8496 kb)

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Sakthivel, K., Watanabe, T. & Nakamoto, H. A small heat-shock protein confers stress tolerance and stabilizes thylakoid membrane proteins in cyanobacteria under oxidative stress. Arch Microbiol 191, 319–328 (2009). https://doi.org/10.1007/s00203-009-0457-z

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  • DOI: https://doi.org/10.1007/s00203-009-0457-z

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