Isolation and sequencing of a 28 kD glutelin-2 gene from maize. common elements in the 5′ flanking regions among zein and glutelin genes

Boronat, Albert; Martínez, M. Carmen; Reina, Manuel; Puigdoménech, Pedro; Palau, Jaume

doi:10.1016/0168-9452(86)90055-5

Cited by 67 publications

(40 citation statements)

References 31 publications

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“…Well-conserved regions (identical residues in three or more proteins) are boxed with solid lines, less well-conserved regions (identical residues in two proteins) with broken lines. (Sequences are taken from [25], [27], [44], [951, [101], [105] 1.,.7 3 subunits of about 70-80 residues regions B and C (Fig. 6a).…”

Section: S Storage Proteinsmentioning

confidence: 99%

The prolamin storage proteins of cereal seeds: structure and evolution

Shewry

Tatham

1990

Biochemical Journal

639

421

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Section: S Storage Proteinsmentioning

confidence: 99%

The prolamin storage proteins of cereal seeds: structure and evolution

Shewry

Tatham

1990

Biochemical Journal

639

421

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“…The complexity of transcriptional regulation for the zein gene family is shown further by the fact that the opaque-2 mutation appears to have little effect on transcription of other gene subfamilies. This is especially evident for the gene encoding the M, 27,000 zein, which shares many of the same conserved sequences in the 5' noncoding region as the genes encoding the a-zeins (Boronat et al, 1986). The recent cloning of opaque-2 locus (Schmidt et al, 1987) should lead to an eventual understanding of how the protein encoded by this locus affects transcription of a-zein genes.…”

Section: Dlscusslonmentioning

confidence: 99%

The opaque-2 Mutation of Maize Differentially Reduces Zein Gene Transcription

Kodrzycki¹,

Boston²

1989

The Plant Cell

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Zeins, the storage proteins of maize seed, are encoded by a large multigene family that is regulated developmentally and expressed in a tissue-specific manner during endosperm development. The synthesis of these proteins is affected by mutations, such as opaque-2, that cause a reduction in the accumulation of zein proteins and mRNAs. We used nuclear run-on transcription assays to analyze the expression of zein genes in developing normal and opaque-2 endosperms and to map the origin of these transcripts with respect to the coding and noncoding regions of the genes. These analyses demonstrate that zein gene expression is regulated transcriptionally and posttranscriptionally in developing endosperm. Transcription of genes encoding a-zeins is inhibited significantly in opaque-2 mutants, with expression of those encoding the M, 22,000 proteins being almost totally blocked. Other gene subfamilies were affected but to a lesser extent.

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“…It is distinct from the main group of maize prolamins, a-zeins, but structurally related to other cereal storage proteins (reviewed in Shewry and Tatham, 1990). The y-zein gene is represented in one or two copies by the haploid maize genome (Boronat et al, 1986), and analysis of cDNA (Prat et al, 1985) and genomic (Boronat et al, 1986) sequences reveals that the protein contains three characteristic structural domains: (1) an N-terminal proline-rich tandem repeat after the signal peptide, (2) a proline-Xaa (P-X) linker domain, and (3) a hydrophobic C-terminal cysteine-rich domain. lmmunocytochemical studies of isolated maize PBs reveal the presence of y-zein surrounding the dense central aggregate of a-zeins (Ludevid et al, 1984).…”

mentioning

confidence: 99%

Two Structural Domains Mediate Two Sequential Events in [gamma]-Zein Targeting: Protein Endoplasmic Reticulum Retention and Protein Body Formation.

1994

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y-Zein is a maize storage protein synthesized by endosperm cells and stored together with a-and P-zeins in specialized organelles called protein bodies. Previous studies have shown that in maize there is only one type of protein body and it is derived directly from the endoplasmic reticulum (ER). In this article, we describe the domains of y-zein involved in ER retention and the domains involved in protein body formation. To identify the signal responsible for y-zein retention in ER-derived protein bodies, DNAs encoding various deletion mutants of y-zein were constructed and introduced into Arabidopsis as a heterologous system. By using pulse-chase experiments and immunoelectron microscopy, we demonstrated that the deletion of a proline-rich domain at the N terminus of y-zein puts an end to its retention in the ER; this resulted in the secretion of the mutated protein. The amino acid sequence of y-zein necessary for ER retention is the repeat domain composed of eight units of the hexapeptide PPPVHL. In addition, we obsenred that only those y-zein mutants that contained both the proline-rich repeat domain and the C-terminal cysteine-rich domain were able to form ER-derived protein bodies. We suggest that the retention of y-zein in the ER could be a result of a protein-protein association or a transient interaction of the repeat domain with ER membranes.

show abstract

Isolation and sequencing of a 28 kD glutelin-2 gene from maize. common elements in the 5′ flanking regions among zein and glutelin genes

Cited by 67 publications

References 31 publications

The prolamin storage proteins of cereal seeds: structure and evolution

The prolamin storage proteins of cereal seeds: structure and evolution

The opaque-2 Mutation of Maize Differentially Reduces Zein Gene Transcription

Two Structural Domains Mediate Two Sequential Events in [gamma]-Zein Targeting: Protein Endoplasmic Reticulum Retention and Protein Body Formation.

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