Protective Roles of Bacterioruberin and Intracellular KCl in the Resistance of Halobacterium salinarium against DNA-damaging Agents.

Shahmohammadi, Hamid Reza; Asgarani, Ezat; Terato, Hiroaki; Saito, Takeshi; Ohyama, Yoshihiko; Gekko, Kunihiko; Yamamoto, Osamu; Ide, Hiroshi

doi:10.1269/jrr.39.251

Cited by 141 publications

(100 citation statements)

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“…In halophilic Archaea, in which membrane lipid composition has been most studied, pigmented carotenoids, in particular bacterioruberins, are major components of the nonpolar lipid pool (243,438). These have been implicated in affording protection from UV-induced damage (390). In addition, many halophilic Archaea also contain retinal as part of bacteriorhodopsin, the purple retinal-containing protein complex that functions as a light-driven proton pump (244).…”

Section: Membrane Lipids Of Archaeamentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

194

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One of the first hurdles to be negotiated in the postgenomic era involves the description of the entire protein content of the cell, the proteome. Such efforts are presently complicated by the various posttranslational modifications that proteins can experience, including glycosylation, lipid attachment, phosphorylation, methylation, disulfide bond formation, and proteolytic cleavage. Whereas these and other posttranslational protein modifications have been well characterized in Eucarya and Bacteria, posttranslational modification in Archaea has received far less attention. Although archaeal proteins can undergo posttranslational modifications reminiscent of what their eucaryal and bacterial counterparts experience, examination of archaeal posttranslational modification often reveals aspects not previously observed in the other two domains of life. In some cases, posttranslational modification allows a protein to survive the extreme conditions often encountered by Archaea. The various posttranslational modifications experienced by archaeal proteins, the molecular steps leading to these modifications, and the role played by posttranslational modification in Archaea form the focus of this review

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Section: Membrane Lipids Of Archaeamentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

194

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“…They are involved in photosynthesis as accessory pigments (2), functioning as antioxidants (3,4), light protection pigments (5,6), and membrane stabilizers (7). Thus far, more than 750 carotenoids have been identified and classified as C 30 , C 40 , and C 50 carotenoids, depending on the number of carbons in their carotene backbones (1).…”

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confidence: 99%

Complete Biosynthetic Pathway of the C₅₀Carotenoid Bacterioruberin from Lycopene in the Extremely Halophilic Archaeon Haloarcula japonica

Yang¹,

Yatsunami²,

Ando³

et al. 2015

J. Bacteriol.

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Haloarcula japonica, an extremely halophilic archaeon that requires high concentrations of NaCl for growth, accumulates the C 50 carotenoid bacterioruberin (BR). By homology analysis, a gene cluster, including c0507, c0506, and c0505, was found and predicted to be involved in the synthesis of bacterioruberin. To elucidate the function of the encoded enzymes, we constructed Ha. japonica mutants of these genes and analyzed carotenoids produced by the mutants. Our research showed that c0507, c0506, and c0505 encoded a carotenoid 3,4-desaturase (CrtD), a bifunctional lycopene elongase and 1,2-hydratase (LyeJ), and a C 50 carotenoid 2؆,3؆-hydratase (CruF), respectively. The above three carotenoid biosynthetic enzymes catalyze the reactions that convert lycopene to bacterioruberin in Ha. japonica. This is the first identification of functional CrtD and CruF in archaea and elucidation of the complete biosynthetic pathway of bacterioruberin from lycopene. IMPORTANCEHaloarcula japonica, an extremely halophilic archaeon, accumulates the C 50 carotenoid bacterioruberin (BR). In this study, we have identified three BR biosynthetic enzymes and have elucidated their functions. Among them, two enzymes were found in an archaeon for the first time. Our results revealed the biosynthetic pathway responsible for production of BR in Ha. japonica and provide a basis for investigating carotenoid biosynthetic pathways in other extremely halophilic archaea. Elucidation of the carotenoid biosynthetic pathway in Ha. japonica may also prove useful for producing the C 50 carotenoid BR efficiently by employing genetically modified haloarchaeal strains.

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“…Alternatively, lycopene may be used as a precursor for bacterioruberins: tetrahydrobisanhydrobacterioruberin, bisanhydrobacterioruberin, and bacterioruberin (22,24). These 50-carbon carotenoids function to increase membrane rigidity (25) and provide protection against UV light (36). Therefore, lycopene is a key intermediate that may be used either for retinal or bacterioruberin biosynthesis (Fig.…”

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confidence: 99%

Bacterioopsin-Mediated Regulation of Bacterioruberin Biosynthesis in Halobacterium salinarum

et al. 2011

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Integral membrane protein complexes consisting of proteins and small molecules that act as cofactors have important functions in all organisms. To form functional complexes, cofactor biosynthesis must be coordinated with the production of corresponding apoproteins. To examine this coordination, we study bacteriorhodopsin (BR), a light-induced proton pump in the halophilic archaeon Halobacterium salinarum. This complex consists of a retinal cofactor and bacterioopsin (BO), the BR apoprotein. To examine possible novel regulatory mechanisms linking BO and retinal biosynthesis, we deleted bop, the gene that encodes BO. bop deletion resulted in a dramatic increase of bacterioruberins, carotenoid molecules that share biosynthetic precursors with retinal. Additional studies revealed that bacterioruberins accumulate in the absence of BO regardless of the presence of retinal or BR, suggesting that BO inhibits bacterioruberin biosynthesis to increase the availability of carotenoid precursors for retinal biosynthesis. To further examine this potential regulatory mechanism, we characterized an enzyme, encoded by the lye gene, that catalyzes bacterioruberin biosynthesis. BO-mediated inhibition of bacterioruberin synthesis appears to be specific to the H. salinarum lye-encoded enzyme, as expression of a lye homolog from Haloferax volcanii, a related archaeon that synthesizes bacterioruberins but lacks opsins, resulted in bacterioruberin synthesis that was not reduced in the presence of BO. Our results provide evidence for a novel regulatory mechanism in which biosynthesis of a cofactor is promoted by apoprotein-mediated inhibition of an alternate biochemical pathway. Specifically, BO accumulation promotes retinal production by inhibiting bacterioruberin biosynthesis.

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Protective Roles of Bacterioruberin and Intracellular KCl in the Resistance of Halobacterium salinarium against DNA-damaging Agents.

Cited by 141 publications

References 20 publications

Posttranslational Protein Modification inArchaea

Posttranslational Protein Modification inArchaea

Complete Biosynthetic Pathway of the C₅₀Carotenoid Bacterioruberin from Lycopene in the Extremely Halophilic Archaeon Haloarcula japonica

Bacterioopsin-Mediated Regulation of Bacterioruberin Biosynthesis in Halobacterium salinarum

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Protective Roles of Bacterioruberin and Intracellular KCl in the Resistance of Halobacterium salinarium against DNA-damaging Agents.

Cited by 141 publications

References 20 publications

Posttranslational Protein Modification inArchaea

Posttranslational Protein Modification inArchaea

Complete Biosynthetic Pathway of the C50Carotenoid Bacterioruberin from Lycopene in the Extremely Halophilic Archaeon Haloarcula japonica

Bacterioopsin-Mediated Regulation of Bacterioruberin Biosynthesis in Halobacterium salinarum

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Complete Biosynthetic Pathway of the C₅₀Carotenoid Bacterioruberin from Lycopene in the Extremely Halophilic Archaeon Haloarcula japonica