Tarantula hemocyanin mRNA

Voit, Renate; Schneider, Hans‐Jürgen

doi:10.1111/j.1432-1033.1986.tb09828.x

Cited by 8 publications

(4 citation statements)

References 44 publications

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“…5. Stereo view of the a-carbon chain tracing of the Panulirus interruptus subunit a hemocyanin showing the location of the splice junctions (11)(12)(13)(14)(15)(16)(17)(18) …”

Section: Discussionmentioning

confidence: 99%

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Characterization of the gene encoding the hemocyanin subunit e from the tarantula Eurypelma californicum.

Voll¹,

Voit²

1990

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

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The gene for the hemocyanin subunit e of the tarantula Eurypelma californicum has been isolated from a genomic phage library by using a corresponding cDNA clone as a probe. The transcriptional unit spans a chromosomal region of about 55 kilobase pairs (kbp). The gene consists ofnine exons that are separated by large introns. The intron/exon boundaries were determined by direct comparison of genomic and cDNA sequences. A putative promoter region ("TATA" box, reversed "CAAT" box) 100 bp 5' to the translational initiation codon strongly suggests the presence of a functional gene. The 3' flanking region carries the polyadenylylation signal (AATAAA) and several conserved structures for the 3' splicing of the pre-mRNA. A comparison of the gene architecture of the subunit e gene with the three-dimensional structure of the arthropod hemocyanin subunit shows a good correspondence with the division of the subunit into three domains (two exons coding for the first, three coding for the second, and four coding for the third domain). The relationship to molluscan hemocyanins, different tyrosinases, and the larval serum proteins is discussed.

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“…5. Stereo view of the a-carbon chain tracing of the Panulirus interruptus subunit a hemocyanin showing the location of the splice junctions (11)(12)(13)(14)(15)(16)(17)(18) …”

Section: Discussionmentioning

confidence: 99%

“…A cDNA library was established from RNA prepared from the total spider heart and screened with a 17-mer oligonucleotide probe corresponding to the amino acid sequences of the CuA oxygen-binding site. The first cDNA clone for an arthropod hemocyanin, termed pHC4, was found to encode the subunit e of Eurypelma hemocyanin (16).…”

mentioning

confidence: 99%

Characterization of the gene encoding the hemocyanin subunit e from the tarantula Eurypelma californicum.

Voll¹,

Voit²

1990

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

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“…Each subunit type has unique immunological and physico-chemical properties but similar oxygenbinding behavior (20,21). Previous work has revealed the amino acid sequences of subunits a, d, and e by conventional protein sequencing methods or by cloning the corresponding cDNAs (22)(23)(24)(25)(26). To understand how structural differentiation and adaptive evolution led to individual subunits obtaining distinct roles requires analysis of the whole primary structure.…”

mentioning

confidence: 99%

Complete Sequence of the 24-mer Hemocyanin of the TarantulaEurypelma californicum

Voit

Feldmaier-Fuchs²,

Schweikardt

et al. 2000

Journal of Biological Chemistry

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Hemocyanins are large oligomeric respiratory proteins found in many arthropods and molluscs. The hemocyanin of the tarantula Eurypelma californicum is a 24-mer protein complex with molecular mass of 1,726,459 Da that consists of seven different polypeptides (a-g), each occupying a distinct position within the native molecule. Here we report the complete molecular structure of the E. californicum hemocyanin as deduced from the corresponding cDNAs. This represents the first complex arthropod hemocyanin to be completely sequenced. The different subunits display 52-66% amino acid sequence identity. Within the subunits, the central domain, which bears the active center with the copper-binding sites A and B, displays the highest degree of identity. Using a homology modeling approach, the putative three-dimensional structure of individual subunits was deduced and compared. Phylogenetic analyses suggest that differentiation of the individual subunits occurred 400 -550 million years ago. The hemocyanin of the stemline Chelicerata was probably a hexamer built up of six distinct subunit types a, b/c, d, e, f, and g, whereas that of the early Arachnida was originally a 24-mer that emerged after the differentiation of subunits b and c.

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“…However, the cDNA and genomic DNA sequences of the e chain of Eurypelma hemocyanin [26,271 indicate that it is synthezised on free ribosomes. This suggests that the site of hemocyanin biosynthesis has varied during the evolution of arthropods.…”

Section: Resultsmentioning

confidence: 99%

Primary structure of hemocyanin subunit c from Panulirus interruptus

Neuteboom

Jekel

Beintema

1992

European Journal of Biochemistry

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The amino acid sequence of the hemocyanin subunit c from the spiny lobster, Panulirus interruptus, has been determined. The elucidation was mainly based on three digests, with CNBr, trypsin and endoproteinase Glu-C, respectively. Additional evidence was obtained by sequencing of peptides from an endoproteinase Lys-C digest. Subunit c is a polypeptide with 661 amino acid residues and with a carbohydrate group attached to residue 476 in the third domain. No heterogeneity was observed. The degree of identity with subunit a is 59%. Some differences with subunit a are an Nterminal extension of six residues, a one-residue C-terminal extension, and a three-residue deletion. Furthermore, carbohydrate attachment is in a different position, as are most half-cystine residues. Limited trypsinolysis resulted in cleavage at the same site as in subunits a and b.Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many molluscs and arthropods. Arthropod hemocyanins consist of hexamers or multihexamers with subunits of about 75 kDa, each of which contains one binuclear copper site The three-dimensional structure of P. interruptus hemocyanin has been determined by X-ray diffraction at a resolution of 0.32 nm, with crystals consisting of a mixture of a and b in roughly equal amounts [6, 71. Each subunit is folded into three domains. The first and the second domain are mainly globular, the third domain contains a sevenstranded P-barrel. The second domain contains the binuclear oxygen-binding site.

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Tarantula hemocyanin mRNA

Cited by 8 publications

References 44 publications

Characterization of the gene encoding the hemocyanin subunit e from the tarantula Eurypelma californicum.

Characterization of the gene encoding the hemocyanin subunit e from the tarantula Eurypelma californicum.

Complete Sequence of the 24-mer Hemocyanin of the TarantulaEurypelma californicum

Primary structure of hemocyanin subunit c from Panulirus interruptus

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