Structure and evolution of Paramecium hemoglobin genes

Yamauchi, Kiyoshi; Tada, Hideo; Usuki, Itaru

doi:10.1016/0167-4781(95)00114-v

Cited by 24 publications

(14 citation statements)

References 23 publications

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“…Although the 5Ј intron is positioned as in 3-on-3 Hbs at position B12.2, the central (ef9.1) and 3Ј (phase 2 in H-helix) introns are in different positions from those of other plant Hb genes (E14.3, G6.3). None of the GLB3 introns correspond to intron positions in the truncated Hbs of Paramecium species or C. eugametos (15)(16)(17).…”

Section: Resultsmentioning

confidence: 99%

A hemoglobin from plants homologous to truncated hemoglobins of microorganisms

Watts

Hunt

Hvitved

et al. 2001

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

186

170

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We have identified a nuclear-encoded Hb from plants (GLB3) that has a central domain similar to the ''truncated'' Hbs of bacteria, protozoa, and algae. The three-dimensional structure of these Hbs is a 2-on-2 arrangement of ␣-helices, distinct from the 3-on-3 arrangement of the standard globin fold [Pesce, A., Couture, M., Dewilde, S., Guertin, M., Yamauchi, K., Ascenzi, P., Moens, L. & Bolognesi, M. (2000) EMBO J. 19, 2424 -2434]. GLB3-like genes are not found in animals or yeast, but our analysis reveals that they are present in a wide range of Angiosperms and a Bryophyte. Although cyanobacteria and Chlamydomonas have 2-on-2 Hbs (GLBN), GLB3 is more likely related to GLBO-type 2-on-2 Hbs from bacteria. Consequently, GLB3 is unlikely to have arisen from a horizontal transfer between the chloroplast and nuclear genomes. Arabidopsis thaliana GLB3 protein exhibits unusual concentration-independent binding of O 2 and CO. The absorbance spectrum of deoxy-GLB3 is unique; the protein forms a transient sixcoordinate structure after reduction and deoxygenation, which slowly converts to a five-coordinate structure. In A. thaliana, GLB3 is expressed throughout the plant but responds to none of the treatments that induce plant 3-on-3 Hbs. Our analysis of the sequence, ligand interactions, and expression profile of GLB3 indicates that this protein has unique biochemical properties, evolutionary history, and, most likely, a function distinct from those of other plant Hbs.

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Section: Resultsmentioning

confidence: 99%

A hemoglobin from plants homologous to truncated hemoglobins of microorganisms

Watts

Hunt

Hvitved

et al. 2001

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

186

170

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“…2a), and Shikama et al [118] suggests that these histidines correspond to distal (E7) and proximal (F8) histidines, respectively. The same types of haemoglobins were sequenced from Tetrahymena pyriformis [54], T. thermophila [119], Paramecium multimicronucleatum, P. triaurelia and P. jenningsi [120]. Two chloroplast haemoglobins from the green alga Chlamydomonas eugametos were sequenced via its cDNA [48].…”

Section: Minihaemoglobins From Prokaryotes and Unicellular Eukaryotesmentioning

confidence: 99%

Evolution of myoglobin

Suzuki

Imai

1998

CMLS, Cell. Mol. Life Sci.

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The distribution, physiological function, amino acid sequence and gene structure of myoglobin and myoglobin-like proteins from various taxa are summarized, and their evolution is discussed. Although it has long been thought that all haemoglobins and myoglobins have evolved from a common ancestral gene, the knowledge presently accumulated about the structures of these proteins suggests that there may be three distinct origins: a 'universal globin', a 'compact globin' and an 'IDO-like globin'.

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“…The standard splice donor and acceptor sequences are present. With the exception of the Paramecium (29 b) and Chironomus (64 b) introns, the G. intestinalis globin introns are short compared with the majority of vertebrate and nonvertebrate globin introns (120 b to 5800 b) (2,17,51,52), suggesting that the intron insertion position, rather than the intron length, may have a functional/evolutionary importance.…”

Section: Sequencing Of G Intestinalis Hb1 and Structuralmentioning

confidence: 99%

Structural, Functional, and Genetic Characterization of Gastrophilus Hemoglobin

Dewilde¹,

Blaxter²,

Hauwaert³

et al. 1998

Journal of Biological Chemistry

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Hemoglobin of Gastrophilus intestinalis (Insecta, Diptera), was purified and characterized. At least two isoforms have been identified by isoelectrofocusing, mass spectrometry, and genomic Southern blotting. Functional studies show a high oxygen affinity due to a low ligand dissociation rate (k off ‫؍‬ 2.4 s ؊1 ) and a relatively high autoxidation rate (t1 ⁄2 ‫؍‬ 1.6/h). The globins were separated under denaturing conditions, and the sequence of Hb1 (M r ‫؍‬ 17,965 ؎ 2) was determined at the protein and DNA level. The open reading frame codes for a polypeptide of 150 amino acids. Although the globin is distantly related to globins from other species, it has a low penalty score against globin templates.Freshly isolated hemoglobin was crystallized from polyethylene glycol. Crystals contain two hemoglobin molecules per asymmetric unit. Solution of the three-dimensional structure by molecular replacement could not be achieved, possibly due to the presence of three protein isoforms in the crystals. In order to determine its threedimensional structure, G. intestinalis Hb1 was overexpressed in Escherichia coli, resulting in a fully functional molecule as confirmed by ligand binding affinity.The globin gene contains two introns at positions D7.0 and G7.0. The D7.0 intron is unprecedented, suggesting that globin gene evolution is much more complex than originally thought.

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Structure and evolution of Paramecium hemoglobin genes

Cited by 24 publications

References 23 publications

A hemoglobin from plants homologous to truncated hemoglobins of microorganisms

A hemoglobin from plants homologous to truncated hemoglobins of microorganisms

Evolution of myoglobin

Structural, Functional, and Genetic Characterization of Gastrophilus Hemoglobin

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