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Photosynth Res. 2018 Jul;137(1):29-39. doi: 10.1007/s11120-017-0475-7. Epub 2017 Dec 26.

Binding of pigments to the cyanobacterial high-light-inducible protein HliC.

Author information

1
Centre Algatech, Institute of Microbiology, Academy of Sciences of the Czech Republic, 379 81, Třeboň, Czech Republic.
2
Faculty of Science, University of South Bohemia, 370 01, České Budějovice, Czech Republic.
3
Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
4
Centre Algatech, Institute of Microbiology, Academy of Sciences of the Czech Republic, 379 81, Třeboň, Czech Republic. sobotka@alga.cz.
5
Faculty of Science, University of South Bohemia, 370 01, České Budějovice, Czech Republic. sobotka@alga.cz.

Abstract

Cyanobacteria possess a family of one-helix high-light-inducible proteins (HLIPs) that are widely viewed as ancestors of the light-harvesting antenna of plants and algae. HLIPs are essential for viability under various stress conditions, although their exact role is not fully understood. The unicellular cyanobacterium Synechocystis sp. PCC 6803 contains four HLIPs named HliA-D, and HliD has recently been isolated in a small protein complex and shown to bind chlorophyll and β-carotene. However, no HLIP has been isolated and characterized in a pure form up to now. We have developed a protocol to purify large quantities of His-tagged HliC from an engineered Synechocystis strain. Purified His-HliC is a pigmented homo-oligomer and is associated with chlorophyll and β-carotene with a 2:1 ratio. This differs from the 3:1 ratio reported for HliD. Comparison of these two HLIPs by resonance Raman spectroscopy revealed a similar conformation for their bound β-carotenes, but clear differences in their chlorophylls. We present and discuss a structural model of HliC, in which a dimeric protein binds four chlorophyll molecules and two β-carotenes.

KEYWORDS:

Chlorophyll; HLIPs; HliC; Raman spectroscopy; Synechocystis; β-Carotene

PMID:
29280045
DOI:
10.1007/s11120-017-0475-7
[Indexed for MEDLINE]

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