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Endosperm transfer cell-specific genes and proteins: structure, function and applications in biotechnology.

Lopato S, Borisjuk N, Langridge P, Hrmova M - Front Plant Sci (2014)

Bottom Line: The success of molecular biology-based approaches to manipulating ETC function is dependent on a thorough understanding of the functions of ETC-specific genes and ETC-specific promoters.The aim of this review is to summarize the existing data on structure and function of ETC-specific genes and their products.Potential applications of ETC-specific genes, and in particular their promoters for biotechnology will be discussed.

View Article: PubMed Central - PubMed

Affiliation: Australian Centre for Plant Functional Genomics, University of Adelaide Glen Osmond, SA, Australia.

ABSTRACT
Endosperm transfer cells (ETC) are one of four main types of cells in endosperm. A characteristic feature of ETC is the presence of cell wall in-growths that create an enlarged plasma membrane surface area. This specialized cell structure is important for the specific function of ETC, which is to transfer nutrients from maternal vascular tissue to endosperm. ETC-specific genes are of particular interest to plant biotechnologists, who use genetic engineering to improve grain quality and yield characteristics of important field crops. The success of molecular biology-based approaches to manipulating ETC function is dependent on a thorough understanding of the functions of ETC-specific genes and ETC-specific promoters. The aim of this review is to summarize the existing data on structure and function of ETC-specific genes and their products. Potential applications of ETC-specific genes, and in particular their promoters for biotechnology will be discussed.

No MeSH data available.


Domain analyses of ZmMRPI-1 and ZmMRPI-2 proteins involved in the two component system (TCS) contain a highly conserved Zinc finger domain in nearly the same location.(A) A sequence alignment of the Zn finger domains, which fold into α-helices. (B) A sequence alignment of the C-terminal DNA-binding domains, which fold into sheets. Protein sequences were aligned with ProMals3D (Pei et al., 2008) and analysed for domain boundaries using SMART (Letunic et al., 2012) and ProDom (Bru et al., 2005). The predicted and consensus secondary structures (ss) are shown in panels (A) and (B) in red (α-helices, h), blue (β-sheets, e) and black (loops) types. Conservation of residues (brown and black types) on a scale of 9–5 is shown at the top of the diagram. (C) Schematics of domain organization of ZmMRPI-1 and ZmMRPI-2, as analysed by SMART (Letunic et al., 2012) and ProDom (Bru et al., 2005). A position of the ATPase, central region-like domain is shown in ZmMRPI-1, while in ZmMRPI-2, glycoprotein E1-like and Raf-like Ras-binding domains are schematically represented. In both entries Zn finger- (light gray) and C-terminal DNA-binding (dark gray) domains are also illustrated. The schematic is drawn to scale of 505 amino acid (aa) residues.
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Figure 4: Domain analyses of ZmMRPI-1 and ZmMRPI-2 proteins involved in the two component system (TCS) contain a highly conserved Zinc finger domain in nearly the same location.(A) A sequence alignment of the Zn finger domains, which fold into α-helices. (B) A sequence alignment of the C-terminal DNA-binding domains, which fold into sheets. Protein sequences were aligned with ProMals3D (Pei et al., 2008) and analysed for domain boundaries using SMART (Letunic et al., 2012) and ProDom (Bru et al., 2005). The predicted and consensus secondary structures (ss) are shown in panels (A) and (B) in red (α-helices, h), blue (β-sheets, e) and black (loops) types. Conservation of residues (brown and black types) on a scale of 9–5 is shown at the top of the diagram. (C) Schematics of domain organization of ZmMRPI-1 and ZmMRPI-2, as analysed by SMART (Letunic et al., 2012) and ProDom (Bru et al., 2005). A position of the ATPase, central region-like domain is shown in ZmMRPI-1, while in ZmMRPI-2, glycoprotein E1-like and Raf-like Ras-binding domains are schematically represented. In both entries Zn finger- (light gray) and C-terminal DNA-binding (dark gray) domains are also illustrated. The schematic is drawn to scale of 505 amino acid (aa) residues.

Mentions: It has been shown that ZmMRP-1 TF binds not only to gene promoters, but it may also bind other proteins (Royo et al., 2009). Two proteins were isolated in a yeast 2-hybrid screen using full length ZmMRP-1 as bait; these were designated as ZmMRP-1 Interactors 1 and 2 (ZmMRPI-1 and ZmMRPI-2; Table 1). Binding of ZmMRP-1 to ZmMRPI-1 and ZmMRPI-2 was confirmed in planta by co-localization of the proteins in transfer cell nuclei. ZmMRPI-1 and ZmMRPI-2 are very similar proteins, both belonging to the C(2)H(2) zinc finger protein subfamily of nuclear proteins. Members of this subfamily interact with MYB-related TF through their C-terminal conserved domains (Royo et al., 2009). In ZmMRPI-1 and ZmMRPI-2 proteins, a Zinc finger domain of the C2H2-type and a C-terminal DNA-binding domain are highly conserved both in disposition and in sequence identities at the amino acid level, which are 89 and 97% for the Zinc finger and DNA-binding domains, respectively (Figure 4). In both proteins the Zinc finger (Figure 4A) and C-terminal DNA-binding (Figure 4B) domains fold into α-helices, and β-sheets, respectively. Although the full-length sequences of ZmMRPI-1 and ZmMRPI-2 share very high sequence identity (85%) and similarity (94%), analysis using the SMART database (Letunic et al., 2012) identified an ATPase, central region-like domain in ZmMRPI-1, but a glycoprotein E1-like domain and putative Raf-like Ras-binding domain in ZmMRPI-2 (Figure 4C). These domains were positioned in different locations of the protein sequences, reflecting localized differences in amino acid sequence that may be important for specific regulatory functions.


Endosperm transfer cell-specific genes and proteins: structure, function and applications in biotechnology.

Lopato S, Borisjuk N, Langridge P, Hrmova M - Front Plant Sci (2014)

Domain analyses of ZmMRPI-1 and ZmMRPI-2 proteins involved in the two component system (TCS) contain a highly conserved Zinc finger domain in nearly the same location.(A) A sequence alignment of the Zn finger domains, which fold into α-helices. (B) A sequence alignment of the C-terminal DNA-binding domains, which fold into sheets. Protein sequences were aligned with ProMals3D (Pei et al., 2008) and analysed for domain boundaries using SMART (Letunic et al., 2012) and ProDom (Bru et al., 2005). The predicted and consensus secondary structures (ss) are shown in panels (A) and (B) in red (α-helices, h), blue (β-sheets, e) and black (loops) types. Conservation of residues (brown and black types) on a scale of 9–5 is shown at the top of the diagram. (C) Schematics of domain organization of ZmMRPI-1 and ZmMRPI-2, as analysed by SMART (Letunic et al., 2012) and ProDom (Bru et al., 2005). A position of the ATPase, central region-like domain is shown in ZmMRPI-1, while in ZmMRPI-2, glycoprotein E1-like and Raf-like Ras-binding domains are schematically represented. In both entries Zn finger- (light gray) and C-terminal DNA-binding (dark gray) domains are also illustrated. The schematic is drawn to scale of 505 amino acid (aa) residues.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3936200&req=5

Figure 4: Domain analyses of ZmMRPI-1 and ZmMRPI-2 proteins involved in the two component system (TCS) contain a highly conserved Zinc finger domain in nearly the same location.(A) A sequence alignment of the Zn finger domains, which fold into α-helices. (B) A sequence alignment of the C-terminal DNA-binding domains, which fold into sheets. Protein sequences were aligned with ProMals3D (Pei et al., 2008) and analysed for domain boundaries using SMART (Letunic et al., 2012) and ProDom (Bru et al., 2005). The predicted and consensus secondary structures (ss) are shown in panels (A) and (B) in red (α-helices, h), blue (β-sheets, e) and black (loops) types. Conservation of residues (brown and black types) on a scale of 9–5 is shown at the top of the diagram. (C) Schematics of domain organization of ZmMRPI-1 and ZmMRPI-2, as analysed by SMART (Letunic et al., 2012) and ProDom (Bru et al., 2005). A position of the ATPase, central region-like domain is shown in ZmMRPI-1, while in ZmMRPI-2, glycoprotein E1-like and Raf-like Ras-binding domains are schematically represented. In both entries Zn finger- (light gray) and C-terminal DNA-binding (dark gray) domains are also illustrated. The schematic is drawn to scale of 505 amino acid (aa) residues.
Mentions: It has been shown that ZmMRP-1 TF binds not only to gene promoters, but it may also bind other proteins (Royo et al., 2009). Two proteins were isolated in a yeast 2-hybrid screen using full length ZmMRP-1 as bait; these were designated as ZmMRP-1 Interactors 1 and 2 (ZmMRPI-1 and ZmMRPI-2; Table 1). Binding of ZmMRP-1 to ZmMRPI-1 and ZmMRPI-2 was confirmed in planta by co-localization of the proteins in transfer cell nuclei. ZmMRPI-1 and ZmMRPI-2 are very similar proteins, both belonging to the C(2)H(2) zinc finger protein subfamily of nuclear proteins. Members of this subfamily interact with MYB-related TF through their C-terminal conserved domains (Royo et al., 2009). In ZmMRPI-1 and ZmMRPI-2 proteins, a Zinc finger domain of the C2H2-type and a C-terminal DNA-binding domain are highly conserved both in disposition and in sequence identities at the amino acid level, which are 89 and 97% for the Zinc finger and DNA-binding domains, respectively (Figure 4). In both proteins the Zinc finger (Figure 4A) and C-terminal DNA-binding (Figure 4B) domains fold into α-helices, and β-sheets, respectively. Although the full-length sequences of ZmMRPI-1 and ZmMRPI-2 share very high sequence identity (85%) and similarity (94%), analysis using the SMART database (Letunic et al., 2012) identified an ATPase, central region-like domain in ZmMRPI-1, but a glycoprotein E1-like domain and putative Raf-like Ras-binding domain in ZmMRPI-2 (Figure 4C). These domains were positioned in different locations of the protein sequences, reflecting localized differences in amino acid sequence that may be important for specific regulatory functions.

Bottom Line: The success of molecular biology-based approaches to manipulating ETC function is dependent on a thorough understanding of the functions of ETC-specific genes and ETC-specific promoters.The aim of this review is to summarize the existing data on structure and function of ETC-specific genes and their products.Potential applications of ETC-specific genes, and in particular their promoters for biotechnology will be discussed.

View Article: PubMed Central - PubMed

Affiliation: Australian Centre for Plant Functional Genomics, University of Adelaide Glen Osmond, SA, Australia.

ABSTRACT
Endosperm transfer cells (ETC) are one of four main types of cells in endosperm. A characteristic feature of ETC is the presence of cell wall in-growths that create an enlarged plasma membrane surface area. This specialized cell structure is important for the specific function of ETC, which is to transfer nutrients from maternal vascular tissue to endosperm. ETC-specific genes are of particular interest to plant biotechnologists, who use genetic engineering to improve grain quality and yield characteristics of important field crops. The success of molecular biology-based approaches to manipulating ETC function is dependent on a thorough understanding of the functions of ETC-specific genes and ETC-specific promoters. The aim of this review is to summarize the existing data on structure and function of ETC-specific genes and their products. Potential applications of ETC-specific genes, and in particular their promoters for biotechnology will be discussed.

No MeSH data available.