Adventitious variability? The amino acid sequences of nonvertebrate globins

Vinogradov, Serge N.; Walz, Daniel A.; Pohajdak, Bill; Moëns, Luc; Kapp, Oscar H.; Suzuki, Tomohiko; Trotman, C. N. A.

doi:10.1016/0305-0491(93)90002-m

Cited by 84 publications

(66 citation statements)

References 240 publications

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“…In contrast to their vertebrate counterparts, the nonvertebrate globins exhibit an extensive variability of their structural organization (1)(2)(3). In bacteria and yeasts, Hbs are found as bifunctional proteins in which the N-terminal globin domain is linked to a second domain with a different activity (see Fig.…”

Section: Hemoglobins (Hbs)mentioning

confidence: 99%

“…The correct chromosomal insertion of the kanMX4 module was verified by PCR amplification using primers specific for the disruption cassette and the chromosome XIV DNA regions flanking the YNL234w gene. 2 For the phenotypic analysis, several dilutions of fresh stationaryphase cultures of mutant strains were spotted together with the corresponding wild-type strains on YP plates (1% yeast extract, 1% bactopeptone) containing different carbon sources (2% glucose, 2% galactose, 3% glycerol). The growth was followed for 5 days at three different temperatures (16,28, and 36°C).…”

Section: Ynl234w Gene Disruption and Phenotypic Testsmentioning

confidence: 99%

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Characterization of a New Hemoprotein in the YeastSaccharomyces cerevisiae

Sartori¹,

Aldegheri²,

Mazzotta³

et al. 1999

Journal of Biological Chemistry

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The Saccharomyces cerevisiae gene YNL234w encodes a 426-amino acid-long protein that shares significant similarities with the globin family. Compared with known globins from unicellular organisms, the Ynl234wp polypeptide is characterized by an unusual structure. In this protein, a central putative heme-binding domain of about 140 amino acids is flanked by two sequences of about 160 and 120 amino acids, respectively, which share no similarity with known polypeptides. Northern analysis indicates that YNL234w transcription is very low in cells grown under normal aerobic conditions but is induced by oxygen-limited growth conditions and by other stress conditions such as glucose repression, heat shock, osmotic stress, and nitrogen starvation. However, the deletion of the gene had no detectable effect on yeast growth. The Ynl234wp polypeptide has been expressed in Escherichia coli, and the hemoprotein nature of the recombinant protein was demonstrated by heme staining after SDS/polyacrylamide gel electrophoresis and spectroscopic analysis. Our data indicate that purified recombinant Ynl234wp possesses a noncovalently bound heme molecule that is predominantly found in a low spin form.

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Section: Hemoglobins (Hbs)mentioning

confidence: 99%

Section: Ynl234w Gene Disruption and Phenotypic Testsmentioning

confidence: 99%

Characterization of a New Hemoprotein in the YeastSaccharomyces cerevisiae

Sartori¹,

Aldegheri²,

Mazzotta³

et al. 1999

Journal of Biological Chemistry

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“…Hemoglobins (Hbs) are ubiquitous proteins found in bacteria, fungi, plants, protozoa, and animals (Vinogradov et al 1993, Bolognesi et al 1997. Plants contain two types of Hbs: the symbiotic and nonsymbiotic (ns) Hbs (Appleby 1992, Andersson et at.…”

Section: Introductionmentioning

confidence: 99%

Nonsymbiotic hemoglobins in rice are synthesized during germination and in differentiating cell types

et al. 2001

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Shearman, L.; Mathiesen, M.; Zhou, Y.J.; Arredondo-Peter, R.; Sarath, Gautam; and Klucas, R. V., "Nonsymbiotic hemoglobins in rice are synthesized during germination and in differentiating cell types" (2001 Abstract: Nonsymbiotic hemoglobins (ns-Hbs) previously have been found in monocots and dicots; however, very little is known about the tissue and cell type localization as well as the physiological function(s) of these oxygen-binding proteins. We report the immunodetection and immunolocalization of ns-Hbs in rice (Oryza sativa L.) by Western blotting and in situ confocal laser scanning techniques. Ns-Hbs were detected in soluble extracts of different tissues from the developing rice seedling by immunoblotting. Levels of ns-Hbs increased in the germinating seed for the fi rst six days following imbibition and remained relatively constant thereafter. In contrast, ns-Hb levels decreased during leaf maturation. Roots and mesocotyls contained detectable, but low levels of ns-Hbs. Split-seed experiments revealed that ns-Hbs are synthesized de novo during seed germination and are expressed in the absence of any signal originating from the embryo. Immunolocalization of ns-Hbs by con-focal microscopy indicated the presence of ns-Hbs primarily in differentiated and differentiating cell types of the developing seedling, such as the aleurone, scutellum, root cap cells, sclerenchyma, and tracheary elements. To our knowledge, this is the fi rst report of the specifi c cellular localization of these proteins during seedling development.

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“…Hemoglobins (Hbs) are heme proteins that have been detected in all phyla, and function by binding and transporting oxygen and other gaseous ligands [1][2][3]. In plants, non-symbiotic Hbs have been detected in organs of vascular and non-vascular species; however, the function of this group of proteins is still not known [4,5].…”

Section: Introductionmentioning

confidence: 99%