Sharp divergence between wheat and barley at loci encoding novel members of the trypsin/α-amylase inhibitors family

  title={Sharp divergence between wheat and barley at loci encoding novel members of the trypsin/$\alpha$-amylase inhibitors family},
  author={P. S{\'a}nchez de la Hoz and Atilio Pedro Castagnaro and Pilar Carbonero},
  journal={Plant Molecular Biology},
Amino acid sequences for three members (CMx1, CMx2, and CMx3) of a new subfamily of trypsin/α-amylase inhibitors in wheat have been deduced from the nucleotide sequences of the corresponding cDNAs. A cDNA clone encoding CMx1 was selected from a wheat developing endosperm library using a probe that encoded barley trypsin inhibitor BTI-CMe at low stringency. Sequences corresponding to CMx2 and CMx3 were obtained from cDNA amplified by the polymerase chain reaction. The three CMx sequences contain… 
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New alpha-amylase and trypsin inhibitors among the CM-proteins of barley (Hordeum vulgare).
N-terminal sequences of proteins CMa, CMb and CMc have been determined and found to be homologous to those previously determined for CMd and CMe, an observation which confirms that their structural genes are members of a dispersed multi-gene family.
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Advances in molecular biology of protein inhibitors from plants have greatly increased knowledge of their structure and "in vitro" properties, and have allowed previously unsuspected relationships between functionally different proteins to be established.