Functional Plant Biology Functional Plant Biology Society
Plant function and evolutionary biology

WM5: Isolation and characterisation of a gene expressed during early meiosis and shoot meristem development in wheat

Chongmei Dong A E , Stephen Thomas B , Dirk Becker C , Horst Lörz C , Ryan Whitford A F , Tim Sutton B , Jason A. Able A G and Peter Langridge B

A Molecular Plant Breeding Cooperative Research Centre, School of Agriculture and Wine, The University of Adelaide, PMB1, Glen Osmond, SA 5064, Australia.

B Australian Centre for Plant Functional Genomics, School of Agriculture and Wine, The University of Adelaide, PMB1, Glen Osmond, SA 5064, Australia.

C Applied Plant Molecular Biology II, University of Hamburg, Ohnhorststrasse 18, D-22609 Hamburg, Germany.

D State Agricultural Biotechnology Centre, Division of Science and Engineering, Murdoch University, Perth, WA 6150, Australia.

E Present address: Plant Breeding Institute, The University of Sydney, PMB11, Camden, NSW 2570, Australia.

F Present address: Department of Plant Systems Biology, VIB / Ghent University, Technology Park 927, B-9052 Ghent, Belgium.

G Corresponding author. Email:

Functional Plant Biology 32(3) 249-258
Submitted: 2 November 2004  Accepted: 10 February 2005   Published: 5 April 2005


Wheat Meiosis 5 (WM5), isolated from an early meiosis anther cDNA library of wheat by cDNA subtraction encodes a novel glycine–serine–proline–alanine-rich protein. The corresponding homologous genes are located on the short arms of chromosomes 3A, 3B and 3D of allohexaploid wheat (Triticum aestivum L.). The copy on 3DS is located within the region deleted in the wheat mutant ph2a that displays increased homoeologous chromosome pairing in crosses with alien species. While WM5 is expressed primarily in young flower buds during early meiosis it is also expressed in shoot meristems, thus indicating functional roles in both meiosis and meristem development. Overall, the WM5 amino acid sequence shares no significant similarity with other known proteins in the NCBI database. However, the carboxyl-terminal region does have similarity with the Arabidopsis PDF1 (Protodermal Factor 1) protein. Comparing WM5 and PDF1 reveals that the two proteins share 33% identity and have similar hydropathy plots and predicted secondary structures. In situ immuno-staining locates the protein to the nuclei of pollen mother cells undergoing meiosis and the epidermal layer of the shoot and flower meristem, including the cell wall and cuticle. We propose that the WM5 protein has a role in shoot and flower development within this economically important cereal crop.

Keywords: meiosis, Ph2, shoot meristem, wheat.


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