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  • 1
    Electronic Resource
    Electronic Resource
    Storage-protein hydrolysis and protein-body breakdown in germinatedZea mays L. seeds (1989)
    Springer
    Planta 180 (1989), S. 90-95 
    Details
    ISSN: 1432-2048
    Keywords: Germination (storage protein) ; Glutelin ; Protein body (germination) ; Storage protein ; Zea mays (storage protein)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Storage proteins of maize (Zea mays L.) were studied in germinated seeds, as were the proteins of protein bodies isolated from endosperms at different germination times. Major endosperm storage proteins were degraded in a sequential way, glutelin 2 being hydrolysed faster than zein 1. Immunocytochemical labelling of the different protein bodies using the antisera anti-glutelin 2 and anti-zein 1 indicates that the protein bodies were degraded by progressive hydrolysis from their surface. The digestion of glutelin 2 correlated with the disappearance of the protein-body membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02411414
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  • 2
    Electronic Resource
    Electronic Resource
    Expression of genes for cell-wall proteins in dividing and wounded tissues ofZea mays L. (1990)
    Springer
    Planta 180 (1990), S. 524-529 
    Details
    ISSN: 1432-2048
    Keywords: Cell division ; Cell wall proteins ; Glycoprotein ; Hydroxyproline-rich glycoprotein ; Wounding ; Zea (cell wall proteins)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Hydroxyproline-rich glycoproteins (HRGPs) fromZea mays have been immunolocalized in the cell wall of root tip cells using ultrathin sections and antibodies ellicited against the purified protein. The accumulation of mRNA corresponding to this protein was studied using the cDNA probe. Maximum accumulation of the mRNA was found in tissues with a high proportion of dividing cells such as those in the root tip of young maize seedlings and a close relationship with cellular division was also observed in in-vitro cultures. However, the level of the mRNA in elongating tissues was minimal, as shown by studies carried out on the elongation zones of root tips and coleoptiles. The mRNA was induced by stress conditions, particularly by wounding young leaves and coleoptiles. It is concluded that in maize this group of proline-rich cell-wall proteins accumulates during cell division and not during cell elongation or differentiation, and participates in the stress-response mechanisms of the plant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02411450
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  • 3
    Electronic Resource
    Electronic Resource
    Role of structural domains for maize γ-zein retention in Xenopus oocytes (1994)
    Springer
    Planta 192 (1994), S. 512-518 
    Details
    ISSN: 1432-2048
    Keywords: Protein domain ; Protein targeting ; Storage protein ; Xenopus oocytes (protein secretion) ; Zein ; Zea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In order to examine the role of cysteine (Cys)-rich domains in the accumulation of maize (Zea mays L.) γ-zein within the endoplasmic-reticulum-derived protein bodies, we studied the localization of γ-zein and of two truncated forms of γ-zein in Xenopus laevis oocytes. The two derivatives were constructed from a DNA encoding the γ-zein: one by deletion of the Pro-X linker region (21 amino acids) and the other by deletion of the Cys-rich domain (94 amino acids). In-vitro-synthesized transcripts were injected into oocytes and the distribution of the translation products was then analyzed. The entire γ-zein and both truncated forms of the γ-zein had accumulated efficiently in microsomes and no traces of secretion were observed. We suggest that neither C-terminal Cys-rich nor Pro-X domains are essential for γ-zein retention in oocyte vesicles. Therefore, structural features derived from disulphide bonds are not necessary for γ-zein targeting on the endoplasmic reticulum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00203589
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  • 4
    Electronic Resource
    Electronic Resource
    Lysine-rich c-zeins are secreted in transgenic Arabidopsis plants (1998)
    Springer
    Planta 205 (1998), S. 420-427 
    Details
    ISSN: 1432-2048
    Keywords: Key words:Arabidopsis (protein secretion) ; Lysine-rich γ-zein ; Prolamin (maize) ; Secretory pathway ; Transgenic Arabidopsis ; Zein targeting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. We have previously shown that the maize (Zea mays L.) storage prolamine γ-zein, accumulates in endoplasmic reticulum-derived protein bodies in transgenic plants of Arabidopsis thaliana (L.) ecotype R+P. The retention of γ-zein in the endoplasmic reticulum was found to be mediated by structural features contained in the polypeptide, an N-terminal proline-rich and a C-terminal cysteine-rich domain which were necessary for the correct retention and assembly of γ-zein within protein bodies (M.I. Geli et al., 1994, Plant Cell 6: 1911–1922). In the present work we incorporated in the γ-zein gene lysine-rich coding sequences which were positioned after the N-terminal proline-rich domain and at five amino-acid residues from the C-terminus. The targeting of lysine-rich γ-zeins was analyzed by expression of chimeric genes regulated by the cauliflower mosaic virus (CaMV) 35S promoter in transgenic Arabidopsis plants. The lysine-rich γ-zeins were detected by immunoblotting and we found that these proteins were modified post-translationally to reach their mature form. Subcellular fractionation and immunocytochemical studies demonstrated that glycosylated lysine-rich γ-zeins were secreted to the cell wall of transgenic Arabidopsis leaf cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050339
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  • 5
    Electronic Resource
    Electronic Resource
    Gene sequence, developmental expression, and protein phosphorylation of RAB-17 in maize (1990)
    Springer
    Plant molecular biology 14 (1990), S. 423-432 
    Details
    ISSN: 1573-5028
    Keywords: maize ; ABA-induced gene ; protein phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ABA-induced MA12 cDNA from maize, which encodes a set of highly phosphorylated embryo proteins, was used to isolate the corresponding genomic clone. This gene, called RAB-17 (responsive to ABA), encodes a basic, glycine-rich protein (mol. wt. 17 164) containing a cluster of 8 serine residues, seven of them contiguous. It is a homologue of the rice RAB-21 gene (Mundy J, Chua NH, EMBO J 7; 2279–2286, 1988). Phosphoamino acid analysis of the isolated protein indicates that only the serine residues are phosphorylated and a putative casein-type kinase phosphorylatable sequence was identified in the protein. The pattern of expression and in vivo phosphorylation of the RAB-17 protein was studied during maize embryo germination and in calli of both meristematic or embryonic origin. ABA treatment induced the synthesis of RAB-17 mRNA and protein in calli, however, the RAB-17 proteins were found to be highly phosphorylated only in embryos.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028778
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  • 6
    Electronic Resource
    Electronic Resource
    Lysine-rich modified γ-zeins accumulate in protein bodies of transiently transformed maize endosperms (1997)
    Springer
    Plant molecular biology 34 (1997), S. 139-149 
    Details
    ISSN: 1573-5028
    Keywords: endosperm-specific expression ; lysine-rich γ-zein ; maize endosperm transient transformation ; γ-zein gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract During maize seed development, endosperm cells synthesize large amounts of storage proteins, α-, β, and γ-zeins, which accumulate within endoplasmic reticulum (ER)-derived protein bodies. The absence of lysine in all zein polypeptides results in an imbalance in the amino acid composition of maize seeds. We modified the maize γ-zein gene through the introduction of lysine-rich (Pro-Lys)n coding sequences at different sites of the γ-zein coding sequence. Maize endosperms were transiently transformed by biolistic bombardment with Lys-rich γ-zein constructs under the control of the 1.7 kb γ-zein seed-specific promoter and the cauliflower mosaic virus (CaMV) 35S promoter. When (Pro-Lys)n sequences were inserted contiguous to or in substitution of the Pro-Xaa region of the γ-zein, high levels of protein were observed. In contrast, when (Pro-Lys)n sequences were inserted five residues from the C-terminal, the transcript was present but modified protein was not detected. These results suggest that only an appropriate positioning of Lys-rich inserts leads to the modified molecule displaying correct folding and stability. Subcellular localization analyses and immunoelectron microscopy studies on isolated protein bodies demonstrated that modified γ-zeins accumulate within these organelles and co-localized with endogenous - and γ-zeins. The studies reported here show the feasibility of manipulating the γ-zein gene in order to obtain stable and correctly targeted Lys-rich zeins in maize seeds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005889314967
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  • 7
    Electronic Resource
    Electronic Resource
    The use of two-dimensional gel electrophoresis in the analysis of organ-specific maize proteins (1988)
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 738-741 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Two-dimensional gel electrophoresis with non-equilibrium pH gradient electrophoresis in the first dimension and sodium dodecyl sulfate-polyacrylamide gels in the second dimension has been used for the analysis of organ-specific proteins in maize. The method has been used to study the whole protein pattern of developing organs and adult leaves as well as protein patterns of in vitro translation. Examples of two-dimensional immunoblotting and in vitro translation of endosperm-specific proteins are also shown. Two-dimensional gel electrophoresis appears as an essential analytical step in the identification of organ-specific proteins and for the detection of the protein products related to organ-specific genes identified by other means.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150091109
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