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Binding of pigments to the cyanobacterial high-light-inducible protein HliC
MK. Shukla, MJ. Llansola-Portoles, M. Tichý, AA. Pascal, B. Robert, R. Sobotka,
Language English Country Netherlands
Document type Journal Article
NLK
ProQuest Central
from 1997-01-01 to 1 year ago
Medline Complete (EBSCOhost)
from 2011-01-01 to 1 year ago
Health & Medicine (ProQuest)
from 1997-01-01 to 1 year ago
- MeSH
- Bacterial Proteins chemistry genetics isolation & purification metabolism MeSH
- beta Carotene metabolism MeSH
- Chlorophyll metabolism MeSH
- Protein Multimerization MeSH
- Spectrum Analysis, Raman MeSH
- Recombinant Proteins genetics isolation & purification metabolism MeSH
- Light-Harvesting Protein Complexes genetics metabolism MeSH
- Synechocystis genetics metabolism physiology MeSH
- Publication type
- Journal Article MeSH
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.
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- $a Shukla, Mahendra Kumar $u Centre Algatech, Institute of Microbiology, Academy of Sciences of the Czech Republic, 379 81, Třeboň, Czech Republic. Faculty of Science, University of South Bohemia, 370 01, České Budějovice, Czech Republic.
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- $a 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.
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- $a Sobotka, Roman $u Centre Algatech, Institute of Microbiology, Academy of Sciences of the Czech Republic, 379 81, Třeboň, Czech Republic. sobotka@alga.cz. Faculty of Science, University of South Bohemia, 370 01, České Budějovice, Czech Republic. sobotka@alga.cz.
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