Agmatine is essential for the cell growth of<i>Thermococcus kodakaraensis</i>

Fukuda, Wakao; Morimoto, Nanako; Imanaka, Tadayuki; Fujiwara, Shinsuke

doi:10.1111/j.1574-6968.2008.01303.x

Cited by 55 publications

(36 citation statements)

References 35 publications

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“…Because all archaeal genomes encode a DHS homologue, it can be reasonably assumed that Spd will be required for cell growth in all archaea. It was discovered that Agm is essential for cell growth of Thermococcus kodakaraensis (83) and cannot be substituted by Put or Spd. Subsequently, it was shown that Agm is used to modify a cytidine in the anticodon of archaeal tRNA(Ile) and that the agmatine modification (agmatidine) is essential for decoding AUA (84,85).…”

Section: Polyamines In Archaeamentioning

confidence: 99%

Polyamines in Eukaryotes, Bacteria, and Archaea

Michael

2016

Journal of Biological Chemistry

239

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Polyamines are primordial polycations found in most cells and perform different functions in different organisms. Although polyamines are mainly known for their essential roles in cell growth and proliferation, their functions range from a critical role in cellular translation in eukaryotes and archaea, to bacterial biofilm formation and specialized roles in natural product biosynthesis. At first glance, the diversity of polyamine structures in different organisms appears chaotic; however, biosynthetic flexibility and evolutionary and ecological processes largely explain this heterogeneity. In this review, I discuss the biosynthetic, evolutionary, and physiological processes that constrain or expand polyamine structural and functional diversity.The common feature of diverse polyamines found in eukaryotes, bacteria, and archaea is that they are all derived from amino acids and are positively charged at physiological pH. Structurally, they are mostly linear and flexible aliphatic chains containing two or more amine groups. They include the diamines 1,3-diaminopropane (Dap), 2 1,4-diaminobutane (putrescine, Put), and 1,5-diaminopentane (cadaverine, Cad), triamines sym-norspermidine (Nspd), spermidine (Spd), and sym-homospermidine (Hspd), the uncommon triamines aminopropylcadaverine and aminobutylcadaverine, the tetraamines norspermine (Nspm), spermine (Spm), and thermospermine (Tspm), and the uncommon tetraamine aminopropyl homospermidine (Fig. 1), and a wide range of longer chain polyamines and branched polyamines. This review will cover the distribution and biosynthesis of different polyamines in the three domains of life and will discuss the mechanisms underlying this biosynthetic diversity.

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Section: Polyamines In Archaeamentioning

confidence: 99%

Polyamines in Eukaryotes, Bacteria, and Archaea

Michael

2016

Journal of Biological Chemistry

239

208

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“…Our previous study found that T. kodakarensis PdaD (TK0149) catalyzed the synthesis of agmatine, the first step in polyamine biosynthesis, and was essential for cell growth (32). Agmatine is also a precursor in the synthesis of agmatidine, an agmatine-conjugated cytidine found at the anticodon wobble position of archaeal tRNA Ile (33).…”

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confidence: 99%

“…5A). A pdaD gene encoding arginine decarboxylase, which catalyzes the synthesis of agmatine, is essential for the growth of T. kodakarensis (32). The plasmid pUD2-⌬bpsA::pdaD was introduced into the strain DAD (⌬pyrF ⌬pdaD).…”

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Identification of a Novel Aminopropyltransferase Involved in the Synthesis of Branched-Chain Polyamines in Hyperthermophiles

et al. 2014

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f Longer-and/or branched-chain polyamines are unique polycations found in thermophiles. N 4 -aminopropylspermine is considered a major polyamine in Thermococcus kodakarensis. To determine whether a quaternary branched penta-amine, N 4 -bis(aminopropyl)spermidine, an isomer of N 4 -aminopropylspermine, was also present, acid-extracted cytoplasmic polyamines were analyzed by high-pressure liquid chromatography, gas chromatography (HPLC), and gas chromatography-mass spectrometry. N 4 -bis(aminopropyl)spermidine was an abundant cytoplasmic polyamine in this species. To identify the enzyme that catalyzes N 4 -bis(aminopropyl)spermidine synthesis, the active fraction was concentrated from the cytoplasm and analyzed by linear ion trap-time of flight mass spectrometry with an electrospray ionization instrument after analysis by the MASCOT database. TK0545, TK0548, TK0967, and TK1691 were identified as candidate enzymes, and the corresponding genes were individually cloned and expressed in Escherichia coli. Recombinant forms were purified, and their N 4 -bis(aminopropyl)spermidine synthesis activity was measured. Of the four candidates, TK1691 (BpsA) was found to synthesize N 4 -bis(aminopropyl)spermidine from spermidine via N 4 -aminopropylspermidine. Compared to the wild type, the bpsA-disrupted strain DBP1 grew at 85°C with a slightly longer lag phase but was unable to grow at 93°C. HPLC analysis showed that both N 4 -aminopropylspermidine and N 4 -bis(aminopropyl)spermidine were absent from the DBP1 strain grown at 85°C, demonstrating that the branched-chain polyamine synthesized by BpsA is important for cell growth at 93°C. Sequence comparison to orthologs from various microorganisms indicated that BpsA differed from other known aminopropyltransferases that produce spermidine and spermine. BpsA orthologs were found only in thermophiles, both in archaea and bacteria, but were absent from mesophiles. These findings indicate that BpsA is a novel aminopropyltransferase essential for the synthesis of branched-chain polyamines, enabling thermophiles to grow in high-temperature environments. P olyamines are small, positively charged aliphatic molecules containing more than two amine residues present in almost all living organisms. Putrescine [4], spermidine [34], and spermine [343] are polyamines commonly observed in the cells of various living organisms, from viruses to humans (1-4). Polyamines are important in cell proliferation and cell differentiation (5, 6), as well as contributing to adaptation to various stresses (7). Interestingly, in addition to common polyamines, thermophiles contain two types of unusual polyamines as major polyamines. One type consists of long linear polyamines such as caldopentamine [3333] NH, N,. Because the relative amounts of long/branched-chain polyamines in cells of (hyper)thermophiles were found to increase as growth temperatures increased, these unique polyamines are regarded as supporting the growth of thermophilic microorganisms under high-temperature conditions (18)(19)(20). An in...

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“…Long-and/or branched-chain polyamines are then produced by the addition of the aminopropyl group derived from decarboxylated S-adenosylmethionine. Previously, we revealed that PdaD Tk catalyzed the first step of polyamine biosynthesis and was essential for cell growth (6). The strain DAD, which lacks the gene pdaD Tk , does not grow in medium without agmatine.…”

Section: (Pathway Ii)mentioning

confidence: 99%

“…A complete genome analysis of T. kodakarensis has been performed, and the pathway of polyamine biosynthesis has been predicted ( Fig. 1) (6,7). It has been speculated that putrescine is synthesized from arginine via agmatine by arginine decarboxylase (PdaD Tk ) and agmatine ureohydrolase.…”

Section: (Pathway Ii)mentioning

confidence: 99%

Dual Biosynthesis Pathway for Longer-Chain Polyamines in the Hyperthermophilic Archaeon Thermococcus kodakarensis

et al. 2010

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The open reading frames (ORFs) TK0240, TK0474, and TK0882, annotated as agmatine ureohydrolase genes, were disrupted. Only the TK0882 gene disruptant showed a growth defect at 85°C and 93°C, and the growth was partially retrieved by the addition of spermidine. In the TK0882 gene disruptant, agmatine and N 1 -aminopropylagmatine accumulated in the cytoplasm. Recombinant TK0882 was purified to homogeneity, and its ureohydrolase characteristics were examined. It possessed a 43-fold-higher k cat /K m value for N 1 -aminopropylagmatine than for agmatine, suggesting that TK0882 functions mainly as N 1 -aminopropylagmatine ureohydrolase to produce spermidine. TK0147, annotated as spermidine/spermine synthase, was also studied. The TK0147 gene disruptant showed a remarkable growth defect at 85°C and 93°C. Moreover, large amounts of agmatine but smaller amounts of putrescine accumulated in the disruptant. Purified recombinant TK0147 possessed a 78-fold-higher k cat /K m value for agmatine than for putrescine, suggesting that TK0147 functions primarily as an aminopropyl transferase to produce N 1 -aminopropylagmatine. In T. kodakarensis, spermidine is produced mainly from agmatine via N 1 -aminopropylagmatine. Furthermore, spermine and N 4 -aminopropylspermine were detected in the TK0147 disruptant, indicating that TK0147 does not function to produce spermine and long-chain polyamines.

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Agmatine is essential for the cell growth ofThermococcus kodakaraensis

Cited by 55 publications

References 35 publications

Polyamines in Eukaryotes, Bacteria, and Archaea

Polyamines in Eukaryotes, Bacteria, and Archaea

Identification of a Novel Aminopropyltransferase Involved in the Synthesis of Branched-Chain Polyamines in Hyperthermophiles

Dual Biosynthesis Pathway for Longer-Chain Polyamines in the Hyperthermophilic Archaeon Thermococcus kodakarensis

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