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Titolo:
ADVENTITIOUS VARIABILITY - THE AMINO-ACID-SEQUENCES OF NONVERTEBRATE GLOBINS
Autore:
VINOGRADOV SN; WALZ DA; POHAJDAK B; MOENS L; KAPP OH; SUZUKI T; TROTMAN CNA;
Indirizzi:
WAYNE STATE UNIV,SCH MED,DEPT BIOCHEM DETROIT MI 48201 WAYNE STATE UNIV,SCH MED,DEPT PHYSIOL DETROIT MI 48201 DALHOUSIE UNIV,DEPT BIOL HALIFAX B3H 4J1 NS CANADA UNIV INSTELLING ANTWERP,DEPT BIOCHEM B-2610 WILRIJK BELGIUM UNIV CHICAGO,ENRICO FERMI INST CHICAGO IL 60637 UNIV CHICAGO,DEPT RADIOL CHICAGO IL 60637 KOCHI UNIV,FAC SCI,DEPT BIOL KOCHI 780 JAPAN UNIV OTAGO,DEPT BIOCHEM DUNEDIN NEW ZEALAND
Titolo Testata:
Comparative biochemistry and physiology. B. Comparative biochemistry
fascicolo: 1, volume: 106, anno: 1993,
pagine: 1 - 26
SICI:
0305-0491(1993)106:1<1:AV-TAO>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYCHAETE TYLORRHYNCHUS-HETEROCHAETUS; CHIRONOMUS-THUMMI-THUMMI; WORM RIFTIA-PACHYPTILA; VENT TUBE WORM; MOLLUSK ANADARA-TRAPEZIA; NEMATODE ASCARIS-SUUM; SEA-CUCUMBER CAUDINA-(MOLPADIA)-ARENICOLA; PARASPONIA-ANDERSONII HEMOGLOBIN; OXYGEN-BINDING FLAVOHEMOPROTEIN; IMMUNOLOGICAL CROSS-REACTIVITY;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
334
Recensione:
Indirizzi per estratti:
Citazione:
S.N. Vinogradov et al., "ADVENTITIOUS VARIABILITY - THE AMINO-ACID-SEQUENCES OF NONVERTEBRATE GLOBINS", Comparative biochemistry and physiology. B. Comparative biochemistry, 106(1), 1993, pp. 1-26

Abstract

1. The more than 140 amino acid sequences of non-vertebrate hemoglobins (Hbs) and myoglobins (Mbs) that are known at present, can be divided into several distinct groups: (1) single-chain globins, containing one heme-binding domain; (2) truncated, single-chain, one-domain globins; (3) chimeric, one-domain globins; (4) chimeric, two-domain globins;and (5) chimeric multi-domain globins. 2. The crystal structures of eight nonvertebrate Hbs and Mbs are known, all of them monomeric, one-domain globin chains. Although these molecules represent plants, prokaryotes and several metazoan groups, and although the inter-subunit interactions in the dimeric and tetrameric molecules differ from the ones observed in vertebrate Hbs, the secondary structures of all seven one-domain globins retain the characteristic vertebrate ''myoglobin fold''. No crystal structures of globins representing the other four groups have been determined. 3. Furthermore, a number of the one-, two- and multi-domain globin chains participate in a broad variety of quaternarystructures, ranging from homo- and heterodimers to highly complex, multisubunit aggregates with M(r) > 3000 kDa (S. N. Vinogradov, Comp. Biochem. Physiol. 82B, 1- 1 5, 1985). 4. (1) The single-chain, single-domain globins are comparable in size to the vertebrate globins and exhibit the widest distribution. (A) Intracellular Hbs include: (i) the monomeric and polymeric Hbs of the polychaete Glycera; (ii) the tetrameric Hb of the echiuran Urechis; (iii) the dimeric Hbs of echinoderms such as Paracaudina and Caudina; and (iv) the dimeric and tetrameric Hbsof molluscs, the bivalves Scapharca, Anadara, Barbatia and Calyptogena. (B) Extracellular Hbs include: (i) the multiple monomeric and dimeric Hbs of the larva of the insect Chironomus; (ii) the Hbs of nematodes such as Trichostrongylus and Caenorhabditis; (iii) the globin chainsforming tetramers and dodecamers and comprising approximately 2/3 of the giant (approximately 3600 kDa), hexagonal bilayer (HBL) Hbs of annelids, e.g. the oligochaete Lumbricus and the polychaete Tylorrhynchusand of the vestimentiferan Lamellibrachia; and (iv) the globin chainscomprising the ca 400 kDa Hbs of Lamellibrachia and the pogonophoran Oligobrachia. (C) Cytoplasmic Hbs include: (i) the Mbs of molluscs, the gastropods Aplysia, Bursatella, Cerithedea, Nassa and Dolabella and the chiton Liolophura; (ii) the three Hb of the symbiont-harboring bivalve Lucina; (iii) the dimeric Hb of the bacterium Vitreoscilla; and (iv) plant Hbs, including the Hbs of symbiont-containing legumes (Lgbs), the Hbs of symbiont-containing non-leguminous plants and the Hbs in the roots of symbiont-free plants. 5. (2) Truncated, single-chain, single-domain globins occur in: (i) the ciliated protozoa Paramecium and Tetrahymena, comprising 116 and 121 residues, respectively; (ii) in the cyanobacterium Nostoc (118 residues) and (iii), in the nemertean Cerebratulus (109 residues). 6. (3) Chimeric greater-than-or-equal-to 40 kDa globins include: (i) the cytoplasmic Hbs in bacteria such as E. coli, Rhizobium and Alcaligenes; and (ii) in the yeasts Saccharomyces and Candida. They have an N-terminal heme-binding domain attached to unrelated proteins with diverse functions and represent, according to Riggs, a previously unrecognized evolutionary pathway for hemoglobin. In the case of Rhizobium, the relationship of the heme-binding domain to other globins is tenuous. The cytoplasmic Hb of the archeopstropod Sulculus has an internal heme-binding domain within a chain of 377 residues, whose sequence cannot be properly aligned with other globins. However, the overall primary structure has a very substantial homology to human indoleamine 2,3-dioxygenase, suggesting that Sulculus Mb is a case of convergent evolution. 7. (4) Chimeric, approximately 40 kDa globins, containing two, covalently linked heme-binding domains, comprise:(i) the extracellular, high-affinity, octameric (approximately 320 kDa) Hbs of parasitic nematodes such as Pseudoterranova and Ascaris; and(ii) the polymeric (ca 430 kDa) intracellular Hb of the clam Barbatia. 8. (5) Chimeric, linear, covalently-linked multi-domain globin sequences are represented so far by the cDNA sequence of one of the two chains comprising the extracellular Hb (approximately 250 kDa) of a crustacean, the brine shrimp Artemia, and consisting of a linear arrangement of nine heme-binding domains linked covalently by 10-20 residue sequences. 9. The giant, extracellular HBL Hbs of annelids and vestimentiferans, appear to consist of large complexes of four chemically distinct, single-domain globins (ca 144 chains), linked together by at least approximately 36 25-28kDa chains which are heme-deficient. The known sequences of linker chains, two from Tylorrhynchus Hb, and one each from Lumbricus and Lamellibrachia Hbs cannot be properly aligned with theknown globin sequences. Furthermore, recent work by Suzuki and Riggs indicates that the gene of one of the Lumbricus linker chains is unrelated to globin genes. 10. In some cases nonvertebrate Hbs exhibit tissue and developmental stage specificity. In several instances such as Chironomus, Glycera and Paramecium, the number of chemically distinct globin chains appears to be much greater than is usually observed amongvertebrate Hbs. In the case of Chironomus, it appears that, despite the presence of normal upstream and downstream regulatory regions, onlya fraction of the large number (> 40) of putative globin genes is expressed at significant levels. Furthermore, although the majority of Chironomus globin genes are intronless, at least one group of its globingenes has introns. 11. The widespread, if episodic occurrence of single-chain Hbs in very diverse groups of eukaryotes and prokaryotes suggests that the Hbs observed at present are likely to have descended from an ancient, monomeric, single-chain, single-domain globin, which existed prior to the time of divergence of prokaryotes and eukaryotes (1500-2000 Myr). This view is consonant with the possibility that globin genes may be ubiquitous though not always expressed (Riggs, Am. Zool. 31, 535-545, 1991; Vinogradov et al., Comp. Biochem. Physiol. 103B, 759-773 1992).

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Documento generato il 28/11/20 alle ore 21:37:56