The cDNA Sequences Encoding the Polymeric Globins of Glycera dibranchiata

Zafar, Rasheeda S.; Chow, Li-Hui; Stern, Mary S.; Walz, Daniel A.

doi:10.1007/978-1-4612-3174-5_31

Cited by 3 publications

(4 citation statements)

References 18 publications

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“…The sequences of G. dibranchiata Hbs have shown that while the polymer Hbs have the normal distal E7His (684,685), the monomeric Hbs have a distal Leu (6, 261, 566) whose presence has been verified by high-resolution crystal structure studies of a monomeric Hb (23,60). The crystal structure shows the typical globin "fold" with no D helix and the heme inserted in the reverse orientation compared with vertebrate hemes, as was observed in Chironomus Hb (511).…”

Section: Annelidsmentioning

confidence: 94%

“…The monomeric Hb has a slightly higher O 2 binding affinity than the polymeric Hb (P 50 ϭ 4 -6 vs. 9 -11 Torr) and lacks cooperativity, whereas the polymeric Hb shows small cooperativity that appears to be due to reversible oxygenation-linked alterations in aggregation (56,391). The two Hbs are synthesized in comparable amounts (483) and were found to consist each of at least half a dozen components (101,285,684,685).…”

Section: Annelidsmentioning

confidence: 99%

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Nonvertebrate Hemoglobins: Functions and Molecular Adaptations

Weber

Vinogradov

2001

Physiological Reviews

453

404

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Hemoglobin (Hb) occurs in all the kingdoms of living organisms. Its distribution is episodic among the nonvertebrate groups in contrast to vertebrates. Nonvertebrate Hbs range from single-chain globins found in bacteria, algae, protozoa, and plants to large, multisubunit, multidomain Hbs found in nematodes, molluscs and crustaceans, and the giant annelid and vestimentiferan Hbs comprised of globin and nonglobin subunits. Chimeric hemoglobins have been found recently in bacteria and fungi. Hb occurs intracellularly in specific tissues and in circulating red blood cells (RBCs) and freely dissolved in various body fluids. In addition to transporting and storing O(2) and facilitating its diffusion, several novel Hb functions have emerged, including control of nitric oxide (NO) levels in microorganisms, use of NO to control the level of O(2) in nematodes, binding and transport of sulfide in endosymbiont-harboring species and protection against sulfide, scavenging of O(2 )in symbiotic leguminous plants, O(2 )sensing in bacteria and archaebacteria, and dehaloperoxidase activity useful in detoxification of chlorinated materials. This review focuses on the extensive variation in the functional properties of nonvertebrate Hbs, their O(2 )binding affinities, their homotropic interactions (cooperativity), and the sensitivities of these parameters to temperature and heterotropic effectors such as protons and cations. Whenever possible, it attempts to relate the ligand binding properties to the known molecular structures. The divergent and convergent evolutionary trends evident in the structures and functions of nonvertebrate Hbs appear to be adaptive in extending the inhabitable environment available to Hb-containing organisms.

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Section: Annelidsmentioning

confidence: 94%

Section: Annelidsmentioning

confidence: 99%

Nonvertebrate Hemoglobins: Functions and Molecular Adaptations

Weber

Vinogradov

2001

Physiological Reviews

453

404

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“…Annelid noncirculating intracellular globins are generally encountered as monomers [9,10], and only the amino‐acid sequences from the polychete, Arenicola marina , [11] and the nucleotide sequence from the polychete, Aphrodite aculeata , [24] have been obtained previously. To date, only cDNA and amino‐acid sequences of circulating intracellular Hb belonging to the marine polychete, Glycera dibranchiata , are known [12,13]. Annelid extracellular hexagonal bilayer hemoglobins (HBL‐Hbs) are assembled into a large multisubunit structure with molecular mass of 3–4 MDa.…”

mentioning

confidence: 99%

Globin gene family evolution and functional diversification in annelids

et al. 2007

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Globins are the most common type of oxygen‐binding protein in annelids. In this paper, we show that circulating intracellular globin (Alvinella pompejana and Glycera dibranchiata), noncirculating intracellular globin (Arenicola marina myoglobin) and extracellular globin from various annelids share a similar gene structure, with two conserved introns at canonical positions B12.2 and G7.0. Despite sequence divergence between intracellular and extracellular globins, these data strongly suggest that these three globin types are derived from a common ancestral globin‐like gene and evolved by duplication events leading to diversification of globin types and derived functions. A phylogenetic analysis shows a distinct evolutionary history of annelid extracellular hemoglobins with respect to intracellular annelid hemoglobins and mollusc and arthropod extracellular hemoglobins. In addition, dehaloperoxidase (DHP) from the annelid, Amphitrite ornata, surprisingly exhibits close phylogenetic relationships to some annelid intracellular globins. We have characterized the gene structure of A. ornata DHP to confirm assumptions about its homology with globins. It appears that it has the same intron position as in globin genes, suggesting a common ancestry with globins. In A. ornata, DHP may be a derived globin with an unusual enzymatic function.

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“…The coelomic erythrocytes of the marine annelid Glycera dibranchiata , commonly named the “blood worm,” contain a mixture of monomeric and polymeric hemoglobins 1–14. Interest in these proteins originated in 1972 when the first primary sequence was published and indicated, by sequence alignment, an exceptional amino acid substitution of His E7† by Leu 15.…”

Section: Introductionmentioning

confidence: 99%

Cushioning the pressure vibration of a zeolite concentrator system using a decoupled balancing duct system

Chang¹,

Lin²

2007

Environ. Prog.

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A honeycomb Zeolite Rotor Concentrator (HZRC) is the main air pollution control device utilized by many semiconductor and optoelectronics manufacturers. Various plant exhaust streams are collected and then transferred to the HZRC for decontamination. In a conventional HZRC, the exhaust fan movement and the switching between different air ducts can cause significant duct pressure variations resulting in production interruption. The minimization of pressure fluctuations to ensure continuous operation of production lines while maintaining a high volatile organic compounds (VOCs) removal efficiency is essential for exhaust treatment in these high technology manufactures. The article introduces a decoupled balancing duct system (DBDS) for controlling the airflows to achieve a balanced pressure in the HZRC system by adding a flow rate control device to the VOCs loaded stream bypass duct of a conventional system. Performance comparisons of HZRC with DBDS and other air flow control systems used by the wafer manufacturers in Hsinchu Science Park, Taiwan are presented. DBDS system had been proved effectively to stabilize the pressure in the airflow ducts, and thus avoided pressure fluctuations; it helped to achieve a high VOCs removal efficiency while ensuring the stability of the HZRC.

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The cDNA Sequences Encoding the Polymeric Globins of Glycera dibranchiata

Cited by 3 publications

References 18 publications

Nonvertebrate Hemoglobins: Functions and Molecular Adaptations

Nonvertebrate Hemoglobins: Functions and Molecular Adaptations

Globin gene family evolution and functional diversification in annelids

Cushioning the pressure vibration of a zeolite concentrator system using a decoupled balancing duct system

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