Cloning and expression analysis of hemoglobin genes from maize (Zea mays ssp. mays) and teosinte (Zea mays ssp. parviglumis)

Aréchaga-Ocampo, Elena; Saenz-Rivera, Juan; Sarath, Gautam; Klucas, Robert V.; Arredondo‐Peter, Raúl

doi:10.1016/s0167-4781(01)00288-3

Cited by 24 publications

(21 citation statements)

References 26 publications

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“…These results were not entirely unexpected, as Arećhaga-Ocampo et al detected maize globin with Western blot in 5−7-day seedlings but found that levels of globin were greatly decreased in 14-day seedlings. 26 Drakakaki et al showed that localization of recombinant proteins contributes to protein functionality. 47 Whereas subcellular localization of the ZmG−GFP protein within the endosperm was not investigated in this study, it was expected to accumulate in the cytoplasm because signal sequences were not used.…”

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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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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“…Although the function of nsHbs is not known, understanding the structural properties of nsHbs will help to clarify the role that these proteins play in plant organs. A maize nshb gene (hbm) has been cloned and characterized [3]. The deduced Hbm amino acid sequence and hydropathy profiles were highly similar to rice Hb1 [3], suggesting that the two proteins should have similar crystal structures.…”

Section: Modeling and General Features Of Hbmmentioning

confidence: 99%

“…A maize nshb gene (hbm) has been cloned and characterized [3]. The deduced Hbm amino acid sequence and hydropathy profiles were highly similar to rice Hb1 [3], suggesting that the two proteins should have similar crystal structures. In order to test this hypothesis, we have used computer tools and rice Hb1 as a template to predict a possible tertiary structure of Hbm.…”

Section: Modeling and General Features Of Hbmmentioning

confidence: 99%

“…The Hbm amino acid sequence [3] and rice Hb1 tertiary structure [15] were obtained from the GenBank database (http://www.ncbi.nlm.nih.gov/GenBank/index) using the accession numbers AAG01375 and 1D8U, respectively. Hbm and rice Hb1 sequences were aligned by using the Cn3D program.…”

Section: Prediction and Modeling Of The Hbm Tertiary Structurementioning

confidence: 99%

“…In this work we have utilized computational methods to predict the tertiary structure of a Hb from maize (Hbm) [3]. Results showed that Hbm and rice Hb1 tertiary structures are almost identical, and suggest that Hbm is a high O 2 -affinity protein whose function might be modulated by binding of regulatory molecules.…”

Section: Introductionmentioning

confidence: 99%

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Modeling the tertiary structure of a maize (Zea mays ssp. mays) non-symbiotic hemoglobin

Saenz-Rivera

Sarath

Arredondo‐Peter

2004

Plant Physiology and Biochemistry

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Modeling the tertiary structure of a maize (Zea mays ssp. mays) nonsymbiotic hemoglobin" (2004 AbstractThe tertiary structure of a maize (Zea mays ssp. mays) non-symbiotic hemoglobin (Hbm) was modeled using computer tools and the known tertiary structure of rice Hb1 as a template. This method was tested by predicting the tertiary structure of soybean leghemoglobin a (Lba) using rice Hb1 as a template. The tertiary structures of the predicted and native Lba were similar, indicating that our computer methods could reliably predict the tertiary structures of plant Hbs. We next predicted the tertiary structure of Hbm. Hbm appears to have a long pre-helix A and a large CD-loop. The positions of the distal and proximal His are identical in Hbm and rice Hb1, which suggests that heme-Fe is hexacoordinate in Hbm and that the kinetic properties of Hbm and rice Hb1 are expected to be very similar, i.e. that Hbm has a high O 2 -affinity. Thermostability analysis showed that Hbm CD-loop is unstable and may provide mobility to amino acids located at the heme pocket for both ligand binding and stabilization and heme-Fe coordination. Analysis of the C-terminal half of Hbm showed the existence of a pocket-like region (the N/C cavity) where interactions with organic molecules or proteins could be possible. Lys K94 protrudes into the N/C cavity, suggesting that K94 may sense the binding of molecules to the N/C cavity. Thus, it is likely that the instability of the CD-loop and the possibility of binding molecules to the N/C cavity are essential for positioning amino acids in the heme pocket and in regulating Hbm activity and function.

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Plant Haemoglobins, Nitrate and Nitric Oxide: Old Players, New Games

Ohwaki

Kaiser

2007

Progress in Botany

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Cloning and expression analysis of hemoglobin genes from maize (Zea mays ssp. mays) and teosinte (Zea mays ssp. parviglumis)

Cited by 24 publications

References 26 publications

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

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

Modeling the tertiary structure of a maize (Zea mays ssp. mays) non-symbiotic hemoglobin

Plant Haemoglobins, Nitrate and Nitric Oxide: Old Players, New Games

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