Transgenic tobacco expressing Vitreoscilla hemoglobin exhibits enhanced growth and altered metabolite production

Holmberg, Niklas; Lilius, Gösta; Bailey, James E.; Bülow, Leif

doi:10.1038/nbt0397-244

Cited by 104 publications

(68 citation statements)

References 27 publications

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“…Transcription of the hemoglobin from the aerobic bacterium Vitreoscilla is elevated under oxygen-limiting conditions (6,7). Heterologous overexpression of the Vitreoscilla globin allows growth to higher cell densities in Escherichia coli and nearly doubles the growth rate of transgenic tobacco, suggesting an ability to increase the availability of intracellular oxygen (8,9). Overexpression of the Vitreoscilla hemoglobin can also rescue E. coli terminal oxidase mutants, indicating that this protein can not only deliver molecular oxygen but also participate in productive electron transport (10).…”

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confidence: 99%

Role for the Salmonella Flavohemoglobin in Protection from Nitric Oxide

Crawford

Goldberg

1998

Journal of Biological Chemistry

164

146

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Hemoglobin homologs are being identified in an expanding number of unicellular prokaryotic and eukaryotic organisms. Many of these hemoglobins are twodomain proteins that possess a flavin-containing reductase in their C terminus. Determination of a function for these flavohemoglobins has been elusive. A Salmonella typhimurium strain harboring a deletion in the flavohemoglobin gene shows no difference in growth under oxidative stress conditions but displays an increased sensitivity to acidified nitrite and S-nitrosothiols, both of which produce nitric oxide. The effect is seen aerobically or anaerobically, indicating that oxygen is not required for flavohemoglobin function. These results suggest a role for the bacterial flavohemoglobins that is independent of oxygen metabolism and provide evidence for a bacterial route of protection from nitric oxide that is distinct from oxidative stress responses.

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confidence: 99%

Role for the Salmonella Flavohemoglobin in Protection from Nitric Oxide

Crawford

Goldberg

1998

Journal of Biological Chemistry

164

146

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“…They are thought to play an important role particularly in aiding plant responses to hypoxia. Holmberg et al (1997) (Li et al, 2005). The overexpression of nsHb1 also protected plants of Arabidopsis thaliana against severe effects of hypoxia, while plants that overexpressed a mutated nsHb1 with low oxygen affinity were just as susceptible to hypoxia as wild type plants (Li et al, 2005).…”

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confidence: 96%

Non-symbiotic hemoglobin and its relation with hypoxic stress

Riquelme¹,

Hinrichsen

2015

Chilean J. Agric. Res.

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Today we know that several types of hemoglobins exist in plants. The symbiotic hemoglobins were discovered in 1939 and are only found in nodules of plants capable of symbiotically fixing atmospheric N. Another class, called non-symbiotic hemoglobin, was discovered 32 yr ago and is now thought to exist throughout the plant kingdom, being expressed in different organs and tissues. Recently the existence of another type of hemoglobin, called truncated hemoglobin, was demonstrated in plants. Although the presence of hemoglobins is widespread in the plant kingdom, their role has not yet been fully elucidated. This review discusses recent findings regarding the role of plant hemoglobins, with special emphasis on their relationship to plants adaptation to hypoxia. It also discusses the role of nitric oxide in plant cells under hypoxic conditions, since one of the functions of hemoglobin appears to be modulating nitric oxide levels in the cells.

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“…It is known that the presence of transgenic hemoglobin can have significant effects on plant growth and can alter concentrations of a wide variety of metabolites. 48,49 However, compartmentalization may compromise heme pyrrole incorporation. It is suggested that the enzymes in plants responsible for heme synthesis and the insertion of iron into heme pyrroles are associated with the mitochondria and chloroplasts, 50−52 but it is not currently clear where heme pyrrole insertion into globin takes place.…”

Section: ■ Discussionmentioning

confidence: 99%

Iron Bioavailability of Maize Hemoglobin in a Caco-2 Cell Culture Model

Bodnar

Proulx

Scott

et al. 2013

J. Agric. Food Chem.

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Maize (Zea mays) is an important staple crop in many parts of the world but has low iron bioavailability, in part due to its high phytate content. Hemoglobin is a form of iron that is highly bioavailable, and its bioavailability is not inhibited by phytate. It was hypothesized that maize hemoglobin is a highly bioavailable iron source and that biofortification of maize with iron can be accomplished by overexpression of maize globin in the endosperm. Maize was transformed with a gene construct encoding a translational fusion of maize globin and green fluorescent protein under transcriptional control of the maize 27 kDa γ-zein promoter. Iron bioavailability of maize hemoglobin produced in Escherichia coli and of stably transformed seeds expressing the maize globin−GFP fusion was determined using an in vitro Caco-2 cell culture model. Maize flour fortified with maize hemoglobin was found to have iron bioavailability that is not significantly different from that of flour fortified with ferrous sulfate or bovine hemoglobin but is significantly higher than unfortified flour. Transformed maize grain expressing maize globin was found to have iron bioavailability similar to that of untransformed seeds. These results suggest that maize globin produced in E. coli may be an effective iron fortificant, but overexpressing maize globin in maize endosperm may require a different strategy to increase bioavailable iron content in maize KeywordsInterdepartmental Genetics Graduate Program, biofortification, hemoglobin, iron bioavailability, transgenic maize ABSTRACT: Maize (Zea mays) is an important staple crop in many parts of the world but has low iron bioavailability, in part due to its high phytate content. Hemoglobin is a form of iron that is highly bioavailable, and its bioavailability is not inhibited by phytate. It was hypothesized that maize hemoglobin is a highly bioavailable iron source and that biofortification of maize with iron can be accomplished by overexpression of maize globin in the endosperm. Maize was transformed with a gene construct encoding a translational fusion of maize globin and green fluorescent protein under transcriptional control of the maize 27 kDa γ-zein promoter. Iron bioavailability of maize hemoglobin produced in Escherichia coli and of stably transformed seeds expressing the maize globin−GFP fusion was determined using an in vitro Caco-2 cell culture model. Maize flour fortified with maize hemoglobin was found to have iron bioavailability that is not significantly different from that of flour fortified with ferrous sulfate or bovine hemoglobin but is significantly higher than unfortified flour. Transformed maize grain expressing maize globin was found to have iron bioavailability similar to that of untransformed seeds. These results suggest that maize globin produced in E. coli may be an effective iron fortificant, but overexpressing maize globin in maize endosperm may require a different strategy to increase bioavailable iron content in maize.

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Transgenic tobacco expressing Vitreoscilla hemoglobin exhibits enhanced growth and altered metabolite production

Cited by 104 publications

References 27 publications

Role for the Salmonella Flavohemoglobin in Protection from Nitric Oxide

Role for the Salmonella Flavohemoglobin in Protection from Nitric Oxide

Non-symbiotic hemoglobin and its relation with hypoxic stress

Iron Bioavailability of Maize Hemoglobin in a Caco-2 Cell Culture Model

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