A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii

Naparstek, Shai; Guan, Ziqiang; Eichler, Jerry

doi:10.1016/j.bbalip.2012.03.002

Cited by 17 publications

(19 citation statements)

References 43 publications

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“…Recent studies recognized the Hfx. volcanii geranylgeranyl reductase HVO_1799 as being able to reduce this -position isoprene (89). Mass spectrometry analysis revealed not only that Hfx.…”

Section: Pathway Of N-linked Glycosylation In Haloferax Volcaniimentioning

confidence: 99%

“…While no studies specifically targeted the glycosylation of the M. voltae S-layer glycoprotein, 59% coverage of the S-layer glycoprotein was obtained during the course of studies performed on the archaellins. From this work, the tryptic peptide T [75][76][77][78][79][80][81][82][83][84][85][86][87][88][89][90][91] , containing one of the potential N-linked sequons, was shown to indeed bear the 779-Da glycan (111).…”

Section: Pathway Of N-linked Glycosylation In Methanogensmentioning

confidence: 99%

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N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis

Jarrell

Ding

Meyer

et al. 2014

Microbiol Mol Biol Rev

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184

214

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SUMMARY N-glycosylation of proteins is one of the most prevalent posttranslational modifications in nature. Accordingly, a pathway with shared commonalities is found in all three domains of life. While excellent model systems have been developed for studying N-glycosylation in both Eukarya and Bacteria , an understanding of this process in Archaea was hampered until recently by a lack of effective molecular tools. However, within the last decade, impressive advances in the study of the archaeal version of this important pathway have been made for halophiles, methanogens, and thermoacidophiles, combining glycan structural information obtained by mass spectrometry with bioinformatic, genetic, biochemical, and enzymatic data. These studies reveal both features shared with the eukaryal and bacterial domains and novel archaeon-specific aspects. Unique features of N-glycosylation in Archaea include the presence of unusual dolichol lipid carriers, the use of a variety of linking sugars that connect the glycan to proteins, the presence of novel sugars as glycan constituents, the presence of two very different N-linked glycans attached to the same protein, and the ability to vary the N-glycan composition under different growth conditions. These advances are the focus of this review, with an emphasis on N-glycosylation pathways in Haloferax , Methanococcus , and Sulfolobus .

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“…Recent studies recognized the Hfx. volcanii geranylgeranyl reductase HVO_1799 as being able to reduce this -position isoprene (89). Mass spectrometry analysis revealed not only that Hfx.…”

Section: Pathway Of N-linked Glycosylation In Haloferax Volcaniimentioning

confidence: 99%

Section: Pathway Of N-linked Glycosylation In Methanogensmentioning

confidence: 99%

N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis

Jarrell

Ding

Meyer

et al. 2014

Microbiol Mol Biol Rev

Self Cite

184

214

View full text Add to dashboard Cite

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“…One of the GGR homologues from hyperthermophile Archaeoglobus fulgidus is highly specific for menaquinone, and therefore it is supposedly involved in the generation of a C 35 fully saturated side chain of menaquinone-7(14H) [19]. An H. volcanii mutant deficient in the gene of a GGR homologue was shown to abolish the saturation at the x-terminal of dolichol phosphate as well as the full saturation of membrane lipids [20]. Hence, it was concluded that the encoded PR functions as a dolichol x-isoprene unit reductase, although the effects of the gene deletion on the structure of respiratory quinone were not confirmed.…”

Section: Introductionmentioning

confidence: 99%

A novel geranylgeranyl reductase from the methanogenic archaeon Methanosarcina acetivorans displays unique regiospecificity

et al. 2014

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Saturation of a prenyl group to various levels is a frequently observed modification of isoprenoids. The members of the geranylgeranyl reductase family, however, are the only known enzymes responsible for such reductive modifications in archaea. A methanogenic archaeon, Methanosarcina acetivorans, has proteins homologous to phytoene desaturase CrtI, which is the carotenogenic enzyme that catalyzes oxidation/isomerization of phytoene to lycopene, but their function in carotenogenesis is unlikely in a methanogen that does not produce carotenoids. In the present study, we identified one of the homologues, MA1492, as a new type of archaeal geranylgeranyl reductase that is not homologous to known geranylgeranyl reductases. The expression of MA1492 in Escherichia coli cells, which were genetically modified to produce unsaturated archaeal‐type lipids, led to the production of partially saturated lipid derivatives. Furthermore, we analyzed the substrate specificity of recombinant MA1492 via in vitro assays. The LC‐MS, or radio‐TLC, analysis of the reaction products showed that the enzyme was definitely specific to compounds containing C20 geranylgeranyl groups and reduced only one of four double bonds in a geranylgeranyl chain. The GC‐MS analysis of the product from geranylgeraniol confirmed that the reduction selectively occurred on the ω‐terminal double bond. The available crystallographic structure of an orthologue enzyme may explain the reaction mechanism that achieves the substrate specificity and regiospecificity. Database Microbial Genome Database (http://mbgd.genome.ad.jp/), EMBOSS Needle (https://www.ebi.ac.uk/Tools/psa/emboss_needle)

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“…This gene has been annotated as a geranylgeranyl hydrogenase and was selected as a priority gene for its These results imply that TK1836 is involved in lipid biosynthesis, but that it is very unlikely to 5 be a tetraether synthase. Instead, subsequent phylogenetic analysis suggests that TK1836 probably belongs to a dehydrogenase family that has been shown to be prenyl reductases (data not shown) [585,586]. If true, the results obtained for this mutant suggest that the presence of double bonds in the precursor molecule of tetraether lipids is a prerequisite to the formation of tetraether lipids.…”

Section: Discussionmentioning

confidence: 85%

Thermococcus kodakarensis : the key to affordable biohydrogen production

Spaans¹

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A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii

Cited by 17 publications

References 43 publications

N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis

N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis

A novel geranylgeranyl reductase from the methanogenic archaeon Methanosarcina acetivorans displays unique regiospecificity

Thermococcus kodakarensis : the key to affordable biohydrogen production

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