Biosynthesis of the cyanobacterial reserve polymer multi‐L‐arginyl‐poly‐L‐aspartic acid (cyanophycin)

Berg, Holger; Ziegler, K.; Piotukh, Kirill; Baier, Kerstin; Lockau, Wolfgang; Volkmer, Rudolf

doi:10.1046/j.1432-1327.2000.01622.x

Cited by 118 publications

(103 citation statements)

References 43 publications

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“…Interestingly, several unclustered genes are present in these four genomes with predicted functions as "global nitrogen regulator," "nitrogen fixation proteins of unknown function," and "nitrogen regulatory protein P-II 1"; nonetheless, these genes have also been reported in non-heterocyst-forming and nondiazotrophic cyanobacteria (25). The fact that Moorea strains survive up to 8 d under nitrogen deprivation can likely be attributed to the presence of cyanophycin, a multi-Larginyl-poly-L-aspartate nitrogen storage reserve material typical of cyanobacteria (26). Of note, our genomic analysis revealed that each of the Moorea genomes contained one cyanophycin synthetase and at least one cyanophycinase gene.…”

Section: Genome Comparison Among Moorea Strains Reveals Significantmentioning

confidence: 78%

Comparative genomics uncovers the prolific and distinctive metabolic potential of the cyanobacterial genus Moorea

Leão

Castelão

Korobeynikov

et al. 2017

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

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Cyanobacteria are major sources of oxygen, nitrogen, and carbon in nature. In addition to the importance of their primary metabolism, some cyanobacteria are prolific producers of unique and bioactive secondary metabolites. Chemical investigations of the cyanobacterial genus Moorea have resulted in the isolation of over 190 compounds in the last two decades. However, preliminary genomic analysis has suggested that genome-guided approaches can enable the discovery of novel compounds from even well-studied Moorea strains, highlighting the importance of obtaining complete genomes. We report a complete genome of a filamentous tropical marine cyanobacterium, Moorea producens PAL, which reveals that about one-fifth of its genome is devoted to production of secondary metabolites, an impressive four times the cyanobacterial average. Moreover, possession of the complete PAL genome has allowed improvement to the assembly of three other Moorea draft genomes. Comparative genomics revealed that they are remarkably similar to one another, despite their differences in geography, morphology, and secondary metabolite profiles. Gene cluster networking highlights that this genus is distinctive among cyanobacteria, not only in the number of secondary metabolite pathways but also in the content of many pathways, which are potentially distinct from all other bacterial gene clusters to date. These findings portend that future genome-guided secondary metabolite discovery and isolation efforts should be highly productive.

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Section: Genome Comparison Among Moorea Strains Reveals Significantmentioning

confidence: 78%

Comparative genomics uncovers the prolific and distinctive metabolic potential of the cyanobacterial genus Moorea

Leão

Castelão

Korobeynikov

et al. 2017

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

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“…It comprises a polyaspartate backbone with arginine side chains attached via their a-amino group to the b-carboxy group of each aspartate ( Figure 3). It is synthesized by cyanophycin synthetase without the involvement of ribosomes, and deposited as granules (Berg et al, 2000;Oppermann-Sanio and Steinbü -chel, 2002). Although cyanophycin is not a polymer with good material properties, it is of interest mainly as a source of polyaspartate, which could replace the chemically synthesized material used as a super-adsorbant or anti-scalant (Oppermann-Sanio and Steinbü chel, 2002).…”

Section: Non-ribosomally Produced Poly-amino Acidsmentioning

confidence: 99%

Production of renewable polymers from crop plants

Beilen

Poirier²

2008

The Plant Journal

142

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SummaryPlants produce a range of biopolymers for purposes such as maintenance of structural integrity, carbon storage, and defense against pathogens and desiccation. Several of these natural polymers are used by humans as food and materials, and increasingly as an energy carrier. In this review, we focus on plant biopolymers that are used as materials in bulk applications, such as plastics and elastomers, in the context of depleting resources and climate change, and consider technical and scientific bottlenecks in the production of novel or improved materials in transgenic or alternative crop plants. The biopolymers discussed are natural rubber and several polymers that are not naturally produced in plants, such as polyhydroxyalkanoates, fibrous proteins and poly-amino acids. In addition, monomers or precursors for the chemical synthesis of biopolymers, such as 4-hydroxybenzoate, itaconic acid, fructose and sorbitol, are discussed briefly.

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“…Bovine casein (Hammersten grade) was from Merck, bovine serum albumin (BSA) was from Roth (Karlsruhe, Germany), and poly(␣,␤-D/L-aspartic acid) (M r ϭ 11,000) was obtained from Bayer (Leverkusen, Germany). Labeling experiments were performed by enzymatic elongation of the C terminus of a CGP primer (32). L-[U- 14 C]arginine was incorporated into the polymer chain using purified cyanophycin synthetase from Synechocystis sp.…”

Section: Taxonomic Determination With Physiological Tests-motility Andmentioning

confidence: 99%

Isolation of Cyanophycin-degrading Bacteria, Cloning and Characterization of an Extracellular Cyanophycinase Gene (cphE) from Pseudomonas anguilliseptica Strain BI

Obst¹,

Oppermann‐Sanio²,

Luftmann³

et al. 2002

Journal of Biological Chemistry

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Eleven bacteria capable of utilizing cyanophycin (cyanophycin granule polypeptide (CGP)) as a carbon source for growth were isolated. One isolate was taxonomically affiliated as Pseudomonas anguilliseptica strain BI, and the extracellular cyanophycinase (CphE) was studied because utilization of cyanophycin as a carbon source and extracellular cyanophycinases were hitherto not described. CphE was detected in supernatants of CGP cultures and purified from a corresponding culture of strain BI employing chromatography on the anion exchange matrix Q-Sepharose and on an arginineagarose affinity matrix. The mature form of the inducible enzyme consisted of one type of subunit with M r ‫؍‬ 43,000 and exhibited high specificity for CGP, whereas proteins and synthetic polyaspartic acid were not hydrolyzed or were only marginally hydrolyzed. Degradation products of the enzyme reaction were identified as aspartic acid-arginine dipeptides (␤-Asp-Arg) by high performance liquid chromatography and electrospray ionization mass spectrometry. The corresponding gene (cphE, 1254 base pairs) was identified in subclones of a cosmid gene library of strain BI by heterologous active expression in Escherichia coli, and its nucleotide sequence was determined. The enzyme exhibited only 27-28% amino acid sequence identity to intracellular cyanophycinases occurring in cyanobacteria. Analysis of the amino acid sequence of cphE revealed a putative catalytic triad consisting of the motif GXSXG plus a histidine and most probably a glutamate residue. In addition, the strong inhibition of the enzyme by Pefabloc ® and phenylmethylsulfonyl fluoride indicated that the catalytic mechanism of CphE is related to that of serine type proteases. Quantitative analysis on the release of ␤-Asp-Arg dipeptides from C-terminal labeled CGP gave evidence for an exo-degradation mechanism.Cyanophycin (cyanophycin granule polypeptide, CGP) 1 is a naturally occurring poly(amino acid), which is synthesized in most cyanobacteria as nitrogen, carbon, and energy storage compound in the early stationary growth phase (1, 2). The water-insoluble CGP is accumulated intracellularly in the form of membraneless granules (3) and is degraded by the cells when growth is resumed. The backbone of this unique biopolymer consists of ␣-amino-␣-carboxyl-linked L-aspartic acid monomers. Most of the ␤-carboxylic groups are covalently bound to the ␣-amino groups of L-arginine residues (4, 5); in recombinant Escherichia coli expressing cyanobacterial CGP-synthesizing enzymes (see below), a significant fraction of arginine is replaced by lysine (6).Although much information has been obtained concerning the non-ribosomal biosynthesis of CGP, which is catalyzed by the cyanophycin synthetase (CphA; see Ref. 7 and cited references therein), only a few reports are available on the intracellular degradation of CGP. Intracellular CGP degradation was first observed in crude extracts of soluble proteins prepared from cells of Anabaena cylindrica (5). The corresponding enzyme, cyanophycinase (CphB), was...

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Biosynthesis of the cyanobacterial reserve polymer multi‐L‐arginyl‐poly‐L‐aspartic acid (cyanophycin)

Cited by 118 publications

References 43 publications

Comparative genomics uncovers the prolific and distinctive metabolic potential of the cyanobacterial genus Moorea

Comparative genomics uncovers the prolific and distinctive metabolic potential of the cyanobacterial genus Moorea

Production of renewable polymers from crop plants

Isolation of Cyanophycin-degrading Bacteria, Cloning and Characterization of an Extracellular Cyanophycinase Gene (cphE) from Pseudomonas anguilliseptica Strain BI

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