Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon merolae 10D

Matsuzaki, Motomichi; Misumi, Osami; Shin-I, Tadasu; Maruyama, Shinichiro; Takahara, Manabu; Miyagishima, Shin-ya; Mori, Toshiyuki; Nishida, Keiji; Yagisawa, Fumi; Nishida, Keishin; Yoshida, Yamato; Nishimura, Yoshiki; Nakao, Shunsuke; Tamaki, Kunihiko; Momoyama, Yu; Higashiyama, Tetsuya; Minoda, Ayumi; Sano, Masako; Nomoto, Hisayo; Oishi, Kazuko; Hayashi, Hiroko; Ohta, Fumiko; Nishizaka, Satoko; Haga, Shinobu; Miura, Sachiko; Morishita, Tomomi; Kabeya, Yukihiro; Terasawa, Kimihiro; Suzuki, Yutaka; Ishii, Yasuyaki; Asakawa, Shuichi; Takano, Hiroyoshi; Ohta, Nobuto; Kuroiwa, Haruko; Tanaka, Kan; Shimizu, Nobuyoshi; Sugano, Sumio; Sato, Naoki; Nozaki, Hisayoshi; Ogasawara, Nagahisa; Kohara, Yuji; Kuroiwa, Tsuneyoshi

doi:10.1038/nature02398

Cited by 1,006 publications

(893 citation statements)

References 32 publications

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“…Further support for the absence of a eukaryotetype hexokinase in G. sulphuraria comes from the recently finished genome sequence of the closely related species C. merolae (Matsuzaki et al, 2004). The C. merolae genome does not encode a eukaryotic hexokinase but a glucokinase (CMO276C) that is typically found in bacteria but not in eukaryotic organisms.…”

Section: Photosynthetic and Respiratory Carbon And Energy Metabolismmentioning

confidence: 99%

“…Accordingly, the C. merolae genome (Matsuzaki et al, 2004) encodes only a single putative monosaccharide transporter (putative arabinose permease; CMK066C), indicating that the relatively large number of putative At3gl8830 30210 657 het 1 At3gl8830 23420 600 het 1 At2gl6120 00780 771 aut 2 At2gl6120 29150 463 het 1 At4g36670 26980 662 het 1 At4g02050 26590 557 het 1 At4g 16480 24560 650 het 1 At4g 16480 07820 652 aut 1 At2g43330 29810 591 het 1 At2g35740 The closest Arabidopsis orthologs were determined by BLASTX searches against the AGI protein database.…”

Section: Solute Transporters In G Sulphurariamentioning

confidence: 99%

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EST-analysis of the thermo-acidophilic red microalga Galdieriasulphuraria reveals potential for lipid A biosynthesis and unveils the pathway of carbon export from rhodoplasts

et al. 2004

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When we think of extremophiles, organisms adapted to extreme environments, prokaryotes come to mind first. However, the unicellular red micro-alga Galdieria sulphuraria (Cyanidiales) is a eukaryote that can represent up to 90% of the biomass in extreme habitats such as hot sulfur springs with pH values of 0-4 and temperatures of up to 56°C. This red alga thrives autotrophically as well as heterotrophically on more than 50 different carbon sources, including a number of rare sugars and sugar alcohols. This biochemical versatility suggests a large repertoire of metabolic enzymes, rivaled by few organisms and a potentially rich source of thermo-stable enzymes for biotechnology. The temperatures under which this organism carries out photosynthesis are at the high end of the range for this process, making G. sulphuraria a valuable model for physical studies on the photosynthetic apparatus. In addition, the gene sequences of this living fossil reveal much about the evolution of modern eukaryotes. Finally, the alga tolerates high concentrations of toxic metal ions such as cadmium, mercury, aluminum, and nickel, suggesting potential application in bioremediation. To begin to explore the unique biology of G. sulphuraria, 5270 expressed sequence tags from two different cDNA libraries have been sequenced and annotated. Particular emphasis has been placed on the reconstruction of metabolic pathways present in this organism. For example, we provide evidence for (i) a complete pathway for lipid A biosynthesis; (ii) export of triose-phosphates from rhodoplasts; (iii) and absence of eukaryotic hexokinases. Sequence data and additional information are available at http://genomics.msu.edu/galdieria.

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Section: Photosynthetic and Respiratory Carbon And Energy Metabolismmentioning

confidence: 99%

Section: Solute Transporters In G Sulphurariamentioning

confidence: 99%

EST-analysis of the thermo-acidophilic red microalga Galdieriasulphuraria reveals potential for lipid A biosynthesis and unveils the pathway of carbon export from rhodoplasts

et al. 2004

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“…An obvious evolutionary trend of MIKC c MADS-box genes in plants is the increase in gene family size, ranging from just one gene in Charophycean green algae to about 40 in flowering plants (Kofuji et al, 2003;Tanabe et al, 2005). Because no MIKC c MADS-box genes could be identified in the genomes of the chlorophycean green alga Chlamydomonas reinhardtii (Tanabe et al, 2005) and the red alga Cyanidioschyzon merolae (Matsuzaki et al, 2004), MIKC c MADS-box genes very likely originated in a common ancestor of charophytes and land plants at least 500 million years ago (MYA).…”

Section: Introductionmentioning

confidence: 99%

The MADS-domain protein PPM2 preferentially occurs in gametangia and sporophytes of the moss Physcomitrella patens

Quodt

Faigl

Saedler

et al. 2007

Gene

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To date, the function of MADS-domain transcription factors in non-seed plants remains largely elusive, although a number of genes have been isolated and characterized from a variety of species. In our study we analyzed PPM2, a classical MIKC-type MADS-box gene from the moss Physcomitrella patens, taking advantage of the unique technical properties Physcomitrella offers in terms of efficient homologous recombination. We determined mRNA and protein distribution and performed targeted disruption of the genomic locus for functional analysis of PPM2. Despite weak ubiquitous expression, PPM2 protein is mostly found in male and female gametangia and basal parts of developing sporophytes. Therefore, PPM2 seems to function in both the haploid and the diploid phase of the moss life cycle. This situation reflects an evolutionary transition state of gene recruitment from an ancestral gametophytic generation into a derived sporophytic generation which became dominating in tracheophytes. However, a knock-out of the PPM2 gene did not cause visible phenotypical changes in the respective structures. The implications of our findings for the understanding of the evolutionary history of MADS-box transcription factors in plants are discussed.

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“…This may be a characteristic feature of the red algal plasma membrane H + -ATPase as it has the distinctive function to pump out H + against the steep pH gradient across the plasma membrane. A homologous plasma membrane H + -ATPase (98.5% similarity and 90.1% identity) was found in another acido-and thermo-philic primitive red alga, Cyanidioschyzon merolae 10D, which also did not contain the regulatory/auto-inhibitory domain (Matsuzaki et al, 2004). Like Cyanidium, Cyanidioschyzon also inhabits acidic hot springs.…”

Section: Characterization Of Plasma Membrane H + -Atpase In Cyanidiummentioning

confidence: 94%

“…The extremely acidophilic nature of C. caldarium is a common feature of the Cyanidiaceae, a red algal group comprising six species, namely, Galdieria sulphuraria, Galdieria partita, Galdieria daedala, Galdieria maxima, Cyanidium caldarium and Cyanidioschyzon merolae (Albertano et al, 2000;Ciniglia et al, 2004). Among these, the complete genome of G. sulphuraria and C. merolae has been sequenced (Weber et al, 2004;Matsuzaki et al, 2004). C. merolae is distinguished from others by the lack of a rigid cell wall, which enables its cells to be broken down simply by freeze-thawing.…”

Section: Introductionmentioning

confidence: 99%

Mechanisms of Acido-Tolerance and Characteristics of Photosystems in an Acidophilic and Thermophilic Red Alga, Cyanidium Caldarium

Enami

Adachi

Shen

2010

Cellular Origin, Life in Extreme Habitats and Astrobiology

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In this chapter, we describe the mechanisms of acido-tolerance in an acido-and thermo-philic red alga, Cyanidium caldarium. In spite of the extremely acidic environments it inhabits, the intracellular pH of Cyanidium cells is kept neutral by pumping out the protons previously leaked into the cells according to the steep pH gradient. The H + pump is driven by the plasma membrane ATPase, utilizing intracellular ATP produced by both oxidative phosphorylation and cyclic photophosphorylation via photosystem I. We also describe the characteristics and function of the two photosystems, Photosystem I (PSI) and II (PSII) in Cyanidium caldarium in comparison with those of cyanobacteria, other eukaryotic algae and higher plants, based on the crystal structures of the two complexes reported so far.

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Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon merolae 10D

Cited by 1,006 publications

References 32 publications

EST-analysis of the thermo-acidophilic red microalga Galdieriasulphuraria reveals potential for lipid A biosynthesis and unveils the pathway of carbon export from rhodoplasts

EST-analysis of the thermo-acidophilic red microalga Galdieriasulphuraria reveals potential for lipid A biosynthesis and unveils the pathway of carbon export from rhodoplasts

The MADS-domain protein PPM2 preferentially occurs in gametangia and sporophytes of the moss Physcomitrella patens

Mechanisms of Acido-Tolerance and Characteristics of Photosystems in an Acidophilic and Thermophilic Red Alga, Cyanidium Caldarium

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