Theoretical and Applied Genetics

, Volume 81, Issue 5, pp 653–660

Molecular characterization of a low-molecular-weight glutenin cDNA clone from Triticum durum

  • B. G. Cassidy
  • J. Dvorak

DOI: 10.1007/BF00226733

Cite this article as:
Cassidy, B.G. & Dvorak, J. Theoret. Appl. Genetics (1991) 81: 653. doi:10.1007/BF00226733


A full-length, low-molecular-weight (LMW) glutenin cDNA clone, pTdUCD1, has been isolated from a Triticum durum cv ‘Mexicali’ wheat cDNA library. The complete sequence was determined and compared to the LMW glutenin genes that have been isolated from hexaploid wheat, Triticum aestivum. This cDNA codes for a protein of 295 amino acids (33,414 daltons) including a 20-amino acid signal peptide as deduced from the DNA sequence. Northern analysis showed that this cDNA hybridizes to a family of related sequences ranging in length from 1,200 to 1,000 nucleotides. This gene is similar but not identical to previously published LMW glutenin gene sequences. The most striking characteristic of all cloned LMW glutenin genes is the conservation of eight cysteine residues, which could be involved in potential secondary or tertiary structure, disulfide bond interactions. This paper presents a structural map defining distinct regions of the LMW glutenin gene family.

Key words

Low-molecular-weight glutenin subunitWheat seed storage proteins

Copyright information

© Springer-Verlag 1991

Authors and Affiliations

  • B. G. Cassidy
    • 1
  • J. Dvorak
    • 1
  1. 1.Department of Agronomy and Range ScienceUniversity of CaliforniaDavisUSA
  2. 2.The Samuel Roberts Noble FoundationArdmoreUSA