Identification of Sesquiterpene Synthases from<i>Nostoc punctiforme</i>PCC 73102 and<i>Nostoc</i>sp. Strain PCC 7120

Agger, Sean A.; López‐Gallego, Fernando; Hoye, Thomas R.; Schmidt‐Dannert, Claudia

doi:10.1128/jb.00759-08

Cited by 127 publications

(112 citation statements)

References 53 publications

(86 reference statements)

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“…Two such sesquiterpene synthases, Alr4685 and Npun_R3832, of Nostoc sp. PCC 7120 and Nostoc punctiforme PCC 73102, respectively, have previously been characterized in vitro (49). Consistent with these observations, heterologous Streptomyces expression of the corresponding sesquiterpene synthases gave rise to formation of sesquiterpene products.…”

Section: Heterologous Expression Of Genes Encoding Bacterial Terpenesupporting

confidence: 65%

Terpene synthases are widely distributed in bacteria

Yamada

Kuzuyama

Komatsu

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

427

361

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Odoriferous terpene metabolites of bacterial origin have been known for many years. In genome-sequenced Streptomycetaceae microorganisms, the vast majority produces the degraded sesquiterpene alcohol geosmin. Two minor groups of bacteria do not produce geosmin, with one of these groups instead producing other sesquiterpene alcohols, whereas members of the remaining group do not produce any detectable terpenoid metabolites. Because bacterial terpene synthases typically show no significant overall sequence similarity to any other known fungal or plant terpene synthases and usually exhibit relatively low levels of mutual sequence similarity with other bacterial synthases, simple correlation of protein sequence data with the structure of the cyclized terpene product has been precluded. We have previously described a powerful search method based on the use of hidden Markov models (HMMs) and protein families database (Pfam) search that has allowed the discovery of monoterpene synthases of bacterial origin. Using an enhanced set of HMM parameters generated using a training set of 140 previously identified bacterial terpene synthase sequences, a Pfam search of 8,759,463 predicted bacterial proteins from public databases and in-house draft genome data has now revealed 262 presumptive terpene synthases. The biochemical function of a considerable number of these presumptive terpene synthase genes could be determined by expression in a specially engineered heterologous Streptomyces host and spectroscopic identification of the resulting terpene products. In addition to a wide variety of terpenes that had been previously reported from fungal or plant sources, we have isolated and determined the complete structures of 13 previously unidentified cyclic sesquiterpenes and diterpenes.terpene synthase | bacteria | heterologous expression

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Section: Heterologous Expression Of Genes Encoding Bacterial Terpenesupporting

confidence: 65%

Terpene synthases are widely distributed in bacteria

Yamada

Kuzuyama

Komatsu

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

427

361

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“…S9). The most abundant corresponds to the newly discovered bacteriocin family (30,31), whereas the terpenes (32) are present in almost all of the 126 genomes. Even the genes encoding cyanobactins (33) were recovered from 10% of the dataset.…”

Section: Prochlorococcus Marinus Mit 9215mentioning

confidence: 99%

Improving the coverage of the cyanobacterial phylum using diversity-driven genome sequencing

Shih

Latifi

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

720

878

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The cyanobacterial phylum encompasses oxygenic photosynthetic prokaryotes of a great breadth of morphologies and ecologies; they play key roles in global carbon and nitrogen cycles. The chloroplasts of all photosynthetic eukaryotes can trace their ancestry to cyanobacteria. Cyanobacteria also attract considerable interest as platforms for "green" biotechnology and biofuels. To explore the molecular basis of their different phenotypes and biochemical capabilities, we sequenced the genomes of 54 phylogenetically and phenotypically diverse cyanobacterial strains. Comparison of cyanobacterial genomes reveals the molecular basis for many aspects of cyanobacterial ecophysiological diversity, as well as the convergence of complex morphologies without the acquisition of novel proteins. This phylum-wide study highlights the benefits of diversity-driven genome sequencing, identifying more than 21,000 cyanobacterial proteins with no detectable similarity to known proteins, and foregrounds the diversity of lightharvesting proteins and gene clusters for secondary metabolite biosynthesis. Additionally, our results provide insight into the distribution of genes of cyanobacterial origin in eukaryotic nuclear genomes. Moreover, this study doubles both the amount and the phylogenetic diversity of cyanobacterial genome sequence data. Given the exponentially growing number of sequenced genomes, this diversity-driven study demonstrates the perspective gained by comparing disparate yet related genomes in a phylum-wide context and the insights that are gained from it.

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“…Germacradienol/geosmin synthase is atypical in that it consists of two terpene cyclase domains. Typical singledomain SCs characterized from Streptomyces and Nostoc include those involved in the synthesis of pentalenene, epi-isozizaene, avermitilol, germacrene A, 8a-epi-␣-selinene, (Ϫ)-␦-cadinene, and (ϩ)-T-muurolol (7)(8)(9)(10)(11)(12)(13). However, recent genome sequencing projects have revealed a large number of potential bacterial SC genes.…”

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confidence: 99%

Characterization of a Novel Sesquiterpene Cyclase Involved in (+)-Caryolan-1-ol Biosynthesis in Streptomyces griseus

Nakano

Horinouchi²,

Ohnishi

2011

Journal of Biological Chemistry

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Most terpenoids have been isolated from plants and fungi and only a few from bacteria. However, an increasing number of genome sequences indicate that bacteria possess a variety of terpenoid cyclase genes. We characterized a sesquiterpene cyclase gene (SGR2079, named gcoA) found in Streptomyces griseus. When expressed in Streptomyces lividans, gcoA directed production of a sesquiterpene, isolated and determined to be (؉)-caryolan-1-ol using spectroscopic analyses. (؉)-Caryolan-1-ol was also detected in the crude cell lysate of wild-type S. griseus but not in a gcoA knockout mutant, indicating that GcoA is a genuine (؉)-caryolan-1-ol synthase. Enzymatic properties were characterized using N-terminally histidine-tagged GcoA, produced in Escherichia coli. As expected, incubation of the recombinant GcoA protein with farnesyl diphosphate yielded (؉)-caryolan-1-ol. However, a small amount of another sesquiterpene was also detected. This was identified as the bicyclic sesquiterpene hydrocarbon (؉)-␤-caryophyllene by comparison with an authentic sample using GC-MS. Incorporation of a deuterium atom into the C-9 methylene of (؉)-caryolan-1-ol in an in vitro GcoA reaction in deuterium oxide indicated that (؉)-caryolan-1-ol was synthesized by a proton attack on the C-8/C-9 double bond of (؉)-␤-caryophyllene. Several ␤-caryophyllene synthases have been identified from plants, but these cannot synthesize caryolan-1-ol. Although caryolan-1-ol has been isolated previously from several plants, the enzyme responsible for its biosynthesis has not been identified previously. GcoA is thus the first known caryolan-1-ol synthase. Isolation of caryolan-1-ol from microorganisms is unprecedented.Terpenoids are the largest family of natural products, including over 24,000 known compounds. They have various biological functions and act as flavorings, pigments, antibiotics, hormones, and antitumor agents. Most terpenoids have been isolated from plants and fungi and only a few from bacteria. All terpenoids are derived from the C 5 precursors isopentenyl diphosphate and dimethylallyl diphosphate. The successive condensation of isopentenyl diphosphate and dimethylallyl diphosphate gives rise to linear isoprenyl diphosphate precursors of various chain lengths, such as geranyl diphosphate (C 10 ), farnesyl diphosphate (FPP, 2 C 15 ), and geranylgeranyl diphosphate (C 20 ). These linear substrates are generally cyclized by terpenoid cyclases to produce the parent skeletons of monoterpenes (C 10 ), sesquiterpenes (C 15 ), diterpenes (C 20 ), and other homologs. Terpenoid cyclases are therefore the first key enzymes in pathways leading to the diverse range of terpenoids. A large number of terpenoid cyclases have been reported from eukaryotes, and these have been studied extensively (1, 2). In contrast, at present there are only a small number of reports of bacterial terpenoid cyclases. Most of the bacterial terpenoid cyclases reported are sesquiterpene cyclases (SCs). Bacterial SCs show no significant amino acid sequence identity with eukaryotic S...

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Identification of Sesquiterpene Synthases fromNostoc punctiformePCC 73102 andNostocsp. Strain PCC 7120

Cited by 127 publications

References 53 publications

Terpene synthases are widely distributed in bacteria

Terpene synthases are widely distributed in bacteria

Improving the coverage of the cyanobacterial phylum using diversity-driven genome sequencing

Characterization of a Novel Sesquiterpene Cyclase Involved in (+)-Caryolan-1-ol Biosynthesis in Streptomyces griseus

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