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Background  Phosphomannomutase (PMM) is an essential enzyme in eukaryotes. However, little is known about  PMM  gene and function in crop plants. Here, we report molecular evolutionary and biochemical analysis of  PMM  genes in bread wheat and related  Triticeae  species.    Results  Two sets of homoeologous  PMM  genes ( TaPMM-1  and  2 ) were found in bread wheat, and two corresponding  PMM  genes were identified in the diploid progenitors of bread wheat and many other diploid  Triticeae  species. The duplication event yielding  PMM-1  and  2  occurred before the radiation of diploid  Triticeae  genomes. The  PMM  gene family in wheat and relatives may evolve largely under purifying selection. Among the six  TaPMM  genes, the transcript levels of  PMM-1  members were comparatively high and their recombinant proteins were all enzymatically active. However,  PMM-2  homoeologs exhibited lower transcript levels, two of which were also inactive. TaPMM-A1, B1 and D1 were probably the main active isozymes in bread wheat tissues. The three isozymes differed from their counterparts in barley and  Brachypodium distachyon  in being more tolerant to elevated test temperatures.    Conclusion  Our work identified the genes encoding PMM isozymes in bread wheat and relatives, uncovered a unique  PMM  duplication event in diverse  Triticeae  species, and revealed the main active PMM isozymes in bread wheat tissues. The knowledge obtained here improves the understanding of  PMM  evolution in eukaryotic organisms, and may facilitate further investigations of  PMM  function in the temperature adaptability of bread wheat.

bmc plant biology

Molecular analysis of phosphomannomutase (PMM) genes reveals a unique PMM duplication event in diverse Triticeae species and the main PMM isozymes in bread wheat tissues