Molecular characterization of a novel methionine-rich delta-kafirin seed storage protein gene in sorghum (Sorghum bicolor L.)

We have isolated, cloned, and characterized a 660 bp full length cDNA encoding a putative seed storage protein gene, delta-kafirin (AY834250), from developing seeds of sorghum (Sorghum bicolor) inbred line SPV-475. Translation of the DNA sequence predicts a 16-kDa polypeptide (precursor) of 147 amin...

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Published inCereal chemistry Vol. 82; no. 6; pp. 706 - 710
Main Authors Izquierdo, L, Godwin, I.D
Format Journal Article
LanguageEnglish
Published St. Paul, MN The American Association of Cereal Chemists, Inc 01.11.2005
American Association of Cereal Chemists
Subjects
alleles
Biological and medical sciences
Cereal and baking product industries
codons
complementary DNA
conserved sequences
Food industries
Fundamental and applied biological sciences. Psychology
gene expression
genetic variation
grain sorghum
inbred lines
kafirins
methionine
molecular sequence data
restriction fragment length polymorphism
reverse transcriptase polymerase chain reaction
Sorghum bicolor
Monocotyledones
Storage protein
Sorghum bicolor
Seeds
Gene
Gramineae
Aminoacid
Angiospermae
Methionine
Spermatophyta
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Summary:We have isolated, cloned, and characterized a 660 bp full length cDNA encoding a putative seed storage protein gene, delta-kafirin (AY834250), from developing seeds of sorghum (Sorghum bicolor) inbred line SPV-475. Translation of the DNA sequence predicts a 16-kDa polypeptide (precursor) of 147 amino acids, rich in methionine residues (17%). Reverse Transcriptase-PCR (RT-PCR) and Real Time-PCR revealed delta-kafirin is only expressed in developing seeds. delta-Kafirin exhibited 96% identity with another methionine-rich sorghum seed storage protein (AY043223). Interestingly, this delta-kafirin gene contained two insertions rich in ATG codons encoding five more methionine residues than AY043223. Comparison of the sorghum delta-kafirin proteins with other seed storage proteins from maize, rice, and Brazil nut revealed conserved domains, mainly at the N-terminus. This similarity, in particular to the zeins, suggests these proteins shared a common ancestor and that the variation observed occurred after the separation of the species.
ISSN:0009-0352
1943-3638
DOI:10.1094/CC-82-0706