Biological distribution of guanidines and phosphagens in marine annelida and related phyla from California, with a note on pluriphosphagens

Robin, Y

doi:10.1016/0010-406x(64)90065-9

Cited by 62 publications

(11 citation statements)

References 28 publications

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“…Most sipunculid species, with the exception of Sipunculus nudus, are known to have dimeric HTK in their musculature as the major phosphagen kinase [2][3][4]11,12,20,21]. We confirmed that the recombinant Siphonosoma HTK with a C-terminal hexameric His-tag is a dimer by analytical size exclusion chromatography (data not shown).…”

Section: Evolutionary Process Of Siphonosoma Htksupporting

confidence: 59%

“…The phosphagen phosphohypotaurocyamine has been observed only in Sipuncula [2][3][4]11], and native HTK has been isolated only from Phascolosoma vulgare [12]. HTK is dimeric, and shows activity for hypotaurocyamine and taurocyamine (the latter activity is about 50% that of hypotaurocyamine) [12], similar to annelid TK, except for the activity for taurocyamine being stronger than that of hypotaurocyamine [12].…”

Section: Introductionmentioning

confidence: 99%

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Hypotaurocyamine kinase evolved from a gene for arginine kinase

2005

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Hypotaurocyamine kinase (HTK) is a member of the highly conserved family of phosphagen kinases that includes creatine kinase (CK) and arginine kinase (AK). HTK is found only in sipunculid worms, and it shows activities for both the substrates hypotaurocyamine and taurocyamine. Determining how HTK evolved in sipunculids is particularly insightful because all sipunculid-allied animals have AK and only some sipunculids have HTK. We determined the cDNA sequence of HTK from the sipunculid worm Siphonosoma cumanense for the first time, cloned it in pMAL plasmid and expressed it in E. coli as a fusion protein with maltose-binding protein. The cDNAderived amino acid sequence of Siphonosoma HTK showed high amino acid identity with molluscan AKs. Nevertheless, the recombinant enzyme of Siphonosoma HTK showed no activity for the substrate arginine, but showed activity for taurocyamine. Comparison of the amino acid sequences of HTK and AK indicated that the amino acid residues necessary for the binding of the substrate arginine in AK have been completely lost in Siphonosoma HTK sequence. The phylogenetic analysis indicated that the HTK amino acid sequence was placed just outside the molluscan AK cluster, which formed a sister group with the arthropod and nematode AKs. These results suggest that Siphonosoma HTK evolved from a gene for molluscan AK. Moreover, to confirm this assertion, we determined by PCR that the gene for Siphonosoma HTK has a 5-exon/4-intron structure, which is homologous with that of the molluscan AK genes. Further, the positions of splice junctions were conserved exactly between the two genes. Thus, we conclude that Siphonosoma HTK has evolved from a primordial gene for molluscan AK.

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Section: Evolutionary Process Of Siphonosoma Htksupporting

confidence: 59%

Section: Introductionmentioning

confidence: 99%

Hypotaurocyamine kinase evolved from a gene for arginine kinase

2005

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“…Lombricine was further found in all terrestrial oligochaetes studied and in several marine polychaetes and echiurids (Thoai and Robin, 1969;Thoai et al, 1972;Robin and Gui11ou, 1980). In contrast with serine from earthworm lomoricine, serine iso1ated from lombricine present in the echiurid Urechis caupo was found to have the L-configuration (Robin, 1964a). OpheLine (52) was iso1ated from the marine po1ychaete Ophe1ia neg1ecta (Thoai et a1., 1963a) and thaLassemine (53) from the echiurid Tha1assema neptuni (Thoai et al, 1972); their structure was established by identification of the hydrolysis products and confirmed by synthesis.…”

Section: Guanidinoethylphosphate Derivativesmentioning

confidence: 91%

“…Octopine (30) (derived from arginine and pyruvic acid) was first isolated from Octopus muscle (Morizawa, 1927) and also found in a large number of molluscs (Mayeda, 1936;Ackermann and Mohr, 1937;Moore and Wilson, 1937;Irvin and Wilson, 1939;Regnouf and Thoai, 1970;Gäde and Zebe, 1973), in yeast cultures (Obata and Iimori, 1952), in sipunculid and nemertean worms (Thoai and Robin, 1969;Robin, 1964a), in sea anemones (Zamit and Newsholme, 1976;Ellington, 1980), and in crown gall tumors induced by Agrobacterium tumefaciens (Menage and Morel, 1964). Homooctopine (31) (derived from homoarginine and pyruvic acid) was isolated from crown gall tumor tissues cultured on media containing homoarginine (Petit and Morel, 1966).…”

Section: Octopine and The Guanidino "Opines"mentioning

confidence: 99%

Natural Guanidino Compounds

Robin¹,

Marescau

1985

Guanidines

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“…With the genomic sequencing project completed, AGAT, GAMT, and CT1 have been investigated in human (Isbrandt and von Figura 1995;Chae et al 1998), other diverse vertebrates such as rat Braissant et al 2005), mouse (Lee et al 1994;Torremans et al 2005), Xenopus (Zhao et al 2001), and zebrafish ) as well as invertebrate tunicate (Roche et al 1957;Robin 1964;Van Pilsum et al 1972;Van Pilsum et al 1975;DeLigio and Ellington 2006). So far, Cr biosynthesis and transport have been established, which are important to the physiology, human pathology, and clinical diagnosis (Wyss and Kaddurah-Daouk 2000;Ellington and Suzuki 2007).…”

Section: Introductionmentioning

confidence: 98%

Characterization of AGAT, GAMT and CT1 in amphioxus: implications for the evolutionary conservation of creatine metabolism related molecules at the invertebrate-to-vertebrate transition

et al. 2008

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In vertebrates, glycine amidinotransferase (AGAT), guanidinoacetate methyltransferase (GAMT), and creatine transporter (CT1) are three proteins involved in creatine synthesis. To provide insight into the molecular evolution mechanism of creatine metabolism, we have cloned and identified BbAGAT, BbGAMT, and BbCT1 homologous genes in amphioxus (Branchiostoma belcheri), whose predicted proteins show high identities with AGAT, GAMT, and CT1 proteins in vertebrates. The phylogenetic analysis indicates that amphioxus AGAT, GAMT, and CT1 are branched off at the base of the vertebrate homologous clade, respectively. Genomic structures of BfAGAT, BfGAMT, and BfCT1 show their comparability with the homologs in vertebrate and original characteristic of cephalochordate, which is consistent with animal classification. To determine the expression patterns of BbAGAT, BbGAMT, and BbCT1, whole-mount and section in situ hybridizations are carried out in embryos and adults of amphioxus. During embryogenesis, they are all expressed mainly in mesendoderm and late somites, but BbCT1 is also expressed in differentiating notochord and digestive tract, as well as in the cytoplasm of zygotes and the blastomeres at cleavage stage. In adult, the transcripts of BbAGAT and BbGAMT are detected in the neural cord, gill, nephridia, endostyle, gut, and gonads, while BbCT1 is expressed mainly in the epithelium of gut. The expression pattern of these three genes is similar to their vertebrate homologs. The result reveals that AGAT, GAMT, and CT1, the primary elements of vertebrate creatine metabolism, exist in cephalochordate amphioxus, and are highly conserved during evolution. It also suggests that similar mechanism of creatine synthesis in vertebrate may occur in amphioxus.

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Biological distribution of guanidines and phosphagens in marine annelida and related phyla from California, with a note on pluriphosphagens

Cited by 62 publications

References 28 publications

Hypotaurocyamine kinase evolved from a gene for arginine kinase

Hypotaurocyamine kinase evolved from a gene for arginine kinase

Natural Guanidino Compounds

Characterization of AGAT, GAMT and CT1 in amphioxus: implications for the evolutionary conservation of creatine metabolism related molecules at the invertebrate-to-vertebrate transition

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