ABSTRACT
We report the isolation and characterization of a cDNA sequence (Mec1) coding for a glutamic acid-rich protein (Pt2L4) from cassava storage roots. Comparative sequence analysis showed a high identity of Pt2L4 with cassava protein C54, which is expressed in vascular tissues of storage roots. Northern blot analysis showed that the Mec1 transcript expression pattern might be related to the maturation of the storage parenchyma cells.
Subject(s)
DNA, Complementary , Glutamic Acid/genetics , Manihot/genetics , Plant Proteins/genetics , Plant Roots/genetics , Amino Acid Sequence , Base Sequence , Glutamic Acid/metabolism , Manihot/metabolism , Molecular Sequence Data , Plant Proteins/biosynthesis , Plant Roots/metabolismABSTRACT
Pearl millet (Pennisetum glaucum L.), a species of the Poaceae family, is an important food crop in Africa, Asia and South America. Its nutritional value is due to storage prolamins accumulated in the seeds. In other species of the same family, the expression of the genes coding for storage prolamins is mediated by the regulatory protein opaque-2. In this paper we show that an opaque-2 -like protein is present in pearl millet too and is expressed during the early stages of seed development. The organization of the gene coding for this protein is similar to that of orthologous genes in other Poaceae species, i.e. six exons separated by five introns. A comparison of amino acid homologies with other described opaque-2 proteins is presented.
Subject(s)
Pennisetum/genetics , Plant Proteins/genetics , Transcription Factors/genetics , Amino Acid Sequence , Cloning, Molecular , Exons/genetics , Gene Expression Regulation, Plant , Genes, Plant/genetics , Introns/genetics , Models, Molecular , Molecular Sequence Data , Phylogeny , Plant Proteins/chemistry , Protein Conformation , RNA, Messenger/genetics , RNA, Messenger/metabolism , Sequence Homology, Amino Acid , Transcription Factors/chemistryABSTRACT
We report the physical-chemical characterization of the major alcohol-soluble proteins present in seeds of pearl millet (Pennisetum glaucum) by SDS-PAGE, bidimensional gel electrophoresis, MALDI-TOF/MS and RP-HPLC. We demonstrate the presence of three major prolamins, called A-, B- and C-pennisetin with mass values around 27, 22 and 12 kDa, respectively. We present partial amino acid sequences of these major proteins, which should allow the posterior isolation of the respective genes.
