Molecular Cloning and Evolution of Lobster Hemocyanin

Kusche, Kristina; Burmester, Thorsten

doi:10.1006/bbrc.2001.4660

Cited by 27 publications

(13 citation statements)

References 24 publications

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“…Sequence similarity between these respiratory proteins was assessed by their comparisons. However, the primary structures of only few representatives of hemocyanins from the subphylum crustacea, namely Macrobrachium nipponense, Homarus americanus, P. interruptus, Palinurus vulgaris, C. magister, and CaSS2 of C. aestuarii, are known (Wang et al 2012;Kusche and Burmester 2001). Structural comparison of crustacean hemocyanin polypeptide chains by sequence alignments (Burmester 2004;Marxen et al 2013) and immunochemistry (Markl et al 1984) showed a discrimination between different subunit types within infraorders.…”

Section: Introductionmentioning

confidence: 99%

Structure and Characterization of Eriphia verrucosa Hemocyanin

et al. 2015

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Arthropod hemocyanins (Hcs) are a family of large extracellular oxygen-transporting proteins with high molecular mass and hexameric or multi-hexameric molecular assembly. This study reports for the first time the isolation and characterization of the structure of an arthropod hemocyanin from crab Eriphia verrucosa (EvH) living in the Black Sea. Its oligomeric quaternary structure is based on different arrangements of a basic 6 × 75 kDa hexameric unit, and four of them (EvH1, EvH2, EvH3, and EvH4) were identified using ion-exchange chromatography. Subunit 3 (EvH3) shows high similarity scores (75.0, 87.5, 91.7, and 75.0 %, respectively) by comparison of the N-terminal sequence of subunit 1 from Cancer pagurus of the North Sea (Cp1), subunits 3 and 6 of Cancer magister (Cm3 and Cm6), and subunit 2 of Carcinus aestuarii (CaSS2), respectively. Moreover, a partial cDNA sequence (1309 bp) of E. verrucosa hemocyanin encoding a protein of 435 amino acids was isolated. The deduced amino acid sequence shows a high degree of similarity with subunits 3, 4, 5, and 6 of C. magister (81-84 %). Most of the hemocyanins are glycosylated, and three putative O-linkage sites were identified in the partial amino acid sequence of EvH at positions 444-446, 478-480, and 547-549, respectively. The higher stability of native Hc in comparison to its subunit EvH4 as determined by circular dichroism (CD) could be explained with the formation of a stabilizing quaternary structure.

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Section: Introductionmentioning

confidence: 99%

Structure and Characterization of Eriphia verrucosa Hemocyanin

et al. 2015

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“…The sequence similarity between these respiratory proteins was assessed by their comparisons. However, the primary structures of only few representatives of hemocyanins from the subphylum crustacea, namely, Macrobrachium nipponense, Homarus americanus, Astacus leptodactylus, P. interruptus, Palinurus vulgaris, C. magister, and CaSS2 of C. aestuarii are known (Wang et al 2012;Schneider et al 1986;Kusche and Burmester 2001). Structural comparison of crustacean hemocyanin polypeptide chains by sequence alignments (Neuteboom et al 1989;Burmester 2004;Marxen et al 2013) and immunochemistry (Markl et al 1984) showed a discrimination between different subunit types within infraorders.…”

Section: Introductionmentioning

confidence: 99%

RETRACTED ARTICLE: Structure and Characterization of Cancer pagurus Hemocyanin

et al. 2014

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“…Phylogenetic analyses show that all three of the P. elephas subunits and the P. interruptus a and b subunits belong to the a-type crustacean hemocyanin sub-family. 4,9,28 Cryoelectron microscopy and 3D-analysis Hemocyanin was purified from the hemolymph of P. elephas by size-exclusion chromatography. The purity of the samples was assessed by native PAGE, SDS-PAGE and negative staining EM.…”

Section: Resultsmentioning

confidence: 99%

“…The P. elephas hemocyanin (PelHc) sequences were manually aligned with a previously published alignment of the arthropod hemocyanin superfamily. 9,28 Hemocyanin purification…”

Section: Materials and Methods Cdna Sequencing And Analysesmentioning

confidence: 99%

Quaternary Structure of the European Spiny Lobster (Palinurus elephas) 1×6-mer Hemocyanin from cryoEM and Amino Acid Sequence Data

Meissner

Stöhr

Kusche

et al. 2003

Journal of Molecular Biology

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Arthropod hemocyanins are large respiratory proteins that are composed of up to 48 subunits (8 £ 6-mer) in the 75 kDa range. A 3D reconstruction of the 1 £ 6-mer hemocyanin from the European spiny lobster Palinurus elephas has been performed from 9970 single particles using cryoelectron microscopy. An 8 Å resolution of the hemocyanin 3D reconstruction has been obtained from about 600 final class averages. Visualisation of structural elements such as a-helices has been achieved. An amino acid sequence alignment shows the high sequence identity (. 80%) of the hemocyanin subunits from the European spiny lobster P. elephas and the American spiny lobster Panulirus interruptus. Comparison of the P. elephas hemocyanin electron microscopy (EM) density map with the known P. interruptus X-ray structure shows a close structural correlation, demonstrating the reliability of both methods for reconstructing proteins. By molecular modelling, we have found the putative locations for the amino acid sequence (597 -605) and the C-terminal end (654 -657), which are absent in the available P. interruptus X-ray data.

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Molecular Cloning and Evolution of Lobster Hemocyanin

Cited by 27 publications

References 24 publications

Structure and Characterization of Eriphia verrucosa Hemocyanin

Structure and Characterization of Eriphia verrucosa Hemocyanin

RETRACTED ARTICLE: Structure and Characterization of Cancer pagurus Hemocyanin

Quaternary Structure of the European Spiny Lobster (Palinurus elephas) 1×6-mer Hemocyanin from cryoEM and Amino Acid Sequence Data

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