Hemocyanins in Spiders, XIX. Complete Amino-Acid Sequence of SubunitdfromEurypelma californicumHemocyanin, and Comparison to Chaine

Schartau, Walter; Eyerle, Friederike; Reisinger, P. W. M.; Geisert, Helga; Storz, Heide; Linzen, Bernt

doi:10.1515/bchm2.1983.364.2.1383

Cited by 69 publications

(22 citation statements)

References 20 publications

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“…The available amino acid sequences from the N-terminal ends of the native polypeptides corroborate this result and show only the removal of the first (initiator) methionine (22)(23)(24). This is consistent with the observation that in chelicerate hemocyanin is synthesized by free ribosomes and subsequently released by cell rupture (38).…”

Section: Resultssupporting

confidence: 88%

“…Sequence analysis revealed that these cDNAs contained open reading frames coding for seven different polypeptides each encompassing the CuA-and CuB-binding sites. 11 of 36 cDNAs were found to code for the known hemocyanin subunits a (24, 26), d (22), and e (23,26). Comparison with partial amino acid sequences of different hemocyanin subunits that had been determined before (37)(38)(39)(40)(41) allowed the unambiguous assignment of the residual open reading frames to subunit b, c, f, and g. Because all these cDNAs represented N-terminally truncated versions missing between 30 and 500 base pairs at the 5Ј end, the corresponding full-length cDNAs were obtained by a polymerase chain reaction-based approach.…”

Section: Resultsmentioning

confidence: 99%

“…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.…”

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confidence: 99%

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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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Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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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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“…(37) Rzoum mecild (trouina) . FPanuirdls baerruq (hemocyanin subunit b) (17) Panns aips (hemocyanin subunit a ) (30) Pamulrus baterrupus (hemocyanin subunit c ) (31) Tachpes rldeAu (hemocyanin subumit a) Ewyp_m calbrcm (hemoyaniln subunit c) (27) Liwuspoyphmus (hemocanin II) (29) Ewuypebn calNornkm (hemocyanin subunit a)(27) Ewypebma califokncm (hmocyanin subunit d) (28) Pac#faacus kelscodus po1pchnoloxdas) (26) Manduca sepa (ewloxddase) Banbyxmon (prophenolaxidase polypepde II) (25) Bombyx mon (prophenoloxidasc polypeptide 1) (25) -Drosoa mkelanogast (prophenoloxidase A1) Amino Acid Sequence Homologies. A search of Swiss-Prot revealed significant sequence similarity of pro-PO A1 to hemocyanins of arthropod (Fig.…”

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confidence: 99%

Nucleotide sequence of the cDNA encoding the proenzyme of phenol oxidase A1 of Drosophila melanogaster.

Fujimoto

Okino

Kawabata

et al. 1995

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

138

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“…Hazes et al (1993), andBeintema et al (1994). Pint a, P interruptus a-chain (Bak and Beintema, 1987), Pint b, P interruptus b-chain (Jekel et al, 1988), and Pint c, R interruptus c-chain (Neuteboom et al, 1992); Eury d, E. ca&rnicurn d-chain (Schartau et al, 1983); Eury e, E. cal4fornicum e-chain and Eury a, E. californicum a-chain (Voit and Feldmaier-Fuchs, 1990); Lim 11, L. pdyphemus subunit I1 (Nakashima et al, 1986); Tachy a, 7: tridenmus a-chain (Nemoto and Takagi, 1983) respectively (LSIMS and LC/ESMS). This association of techniques has been shown to be very efficient for the rapid, reliable and sensitive determination of peptide sequences.…”

Section: E S S K Y S I E S S M Y S I E S S G Y S I E S S H D S I E mentioning

confidence: 99%

Complete Ammo Acid Sequence of the Aa6 Subunit of the Scorpion Androctonus australis Hemocyanin Determined by Edman Degradation and Mass Spectrometry

Buzy

Gagnon

Lamy

et al. 1995

European Journal of Biochemistry

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The primary structure of the hemocyanin Aa6 subunit from the scorpion Androctonus u~istralis was resolved by using protein sequencing and mass spectrometry for analysis of the polypeptide chain and of fragments obtained by CNBr, trypsin, and chymotrypsin cleavage. Due to the high sensitivity of the methodologies used, only a small amount of material, less than 1 mg, was consumed. The complete sequence is composed of 626 amino acid residues and the protein is not glycosylated but probably phosphorylated at Ser374. Its molecular mass measured by mass spectrometry (71 8 9 0 k 7 Da) is about 30 Da higher than the mass calculated from the sequence data (71 860.1 Da). The origin of this difference is not clear but could result from minor molecular heterogeneities. Within the chelicerates, the Aa6 subunit of the arachnid A. uustmlis shares 405 identical residues with chain e of another arachnid, Eurypelrnu calijornicurn, and 399 with chain IX of the merostom Ec1zypleu.q trirleiztatus. The degrees of identity between these three subunits, which are known to occupy the same location in the native hemocyanin oligomers, are significantly higher than those existing between the subunits a, d, and e of E. cal$ornicurn. This favors the hypothesis that gene duplications, leading to separate chains in one species, have occurred before the divergence between arachnids and merostoms.

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Hemocyanins in Spiders, XIX. Complete Amino-Acid Sequence of SubunitdfromEurypelma californicumHemocyanin, and Comparison to Chaine

Cited by 69 publications

References 20 publications

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

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

Nucleotide sequence of the cDNA encoding the proenzyme of phenol oxidase A1 of Drosophila melanogaster.

Complete Ammo Acid Sequence of the Aa6 Subunit of the Scorpion Androctonus australis Hemocyanin Determined by Edman Degradation and Mass Spectrometry

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