Molecular assembly and evolution of multi-subunit extracellular annelid hemoglobins
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概要
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An extracellular annelid hemoglobin is a multi-subunit protein with a molecular weight of 3-4X106 and exhibits a hexagonal bilayer of twelve submultiples. Recent advances in studies on the molecular evolution and assembly of the huge annelid hemoglobins are summarized. Sequence determinations of the eight polypeptide chains of the multi-subunit hemoglobins of the polychaete Tylorrhynchus heterochaetus and the oligochaete Lumbricus terrestris have provided fundamental information on the common molecular architecture and the phylogeny of these huge dioxygen-carrying proteins. In addition, morphological studies using scanning transmission electron microscopy and conventional transmission electron microscopy with image analysis have revealed the tetrahedeal structure of the submultiple. A new nomenclature 'a ', 'A ', 'b ', and 'B ', is proposed for the four basic constituent chains common to oligochaete and polychaete hemoglobins based on their homology. Phylogenetically, these heme-containing chains can be separated into two strains 'A ', and 'B'. According to the symmetrical '192-chain' model, the multi-subunit hemoglobins might be represented as '(aAbB)48'・ The minimum entity 'aAbB ' that consists of a monomeric chain 'a ' and a disulfide-bonded trimer 'AbB' may correspond to one unit in the tetrahedral of the submultiple in electron microscopic appearance. On the basis of recent information, earlier models are evaluated as well as the 'bracelet' model, in which the minor subunits D1 and D2 without heme have a key role in linking the complexes of subunit a and subunit AbB together.
- 社団法人日本動物学会の論文
- 1990-02-15
著者
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Gotoh Toshio
Department of Cardiology, Ashikaga Red Cross Hospital
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Suzuki Tomohiko
Department of Biology, Faculty of Science, Kochi University
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Suzuki Tomohiko
Department Of Biology Faculty Of Science Kochi University
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Gotoh Toshio
Department Of Biology College Of General Education University Of Tokushima
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