The LEA proteins and trehalose loving couple: a step forward in anhydrobiotic engineering.
Adaptation to desiccation tolerance or anhydrobiosis has puzzled scientists for more than 300 years. Over the last few decades, considerable emphasis has been placed on understanding the role of two key molecules involved in anhydrobiosis: a peculiar disaccharide named trehalose and the hydrophilic LEA (Late Embryogenesis Abundant) proteins. In an article published in the Biochemical Journal in 2005, Alan Tunnacliffe and colleagues found that LEA proteins (alone, or more so in combination with trehalose) can protect stress-sensitive enzymes, such as citrate synthase and lactate dehydrogenase, from aggregation due to desiccation and freezing. Upon heat-stress, however, LEA proteins alone cannot prevent these enzymes from aggregating unless trehalose is present. This is the first report that LEA proteins can act as 'molecular shields' to prevent aggregation-induced cell damage due to water loss.
Iturriaga
Gabriel
G
Centro de Investigación en Biotecnología, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, Cuernavaca 62209, Mexico.
D000954:Antigens, Surface / Q000378:metabolism*; D001698:Biomedical Engineering / Q000379:methods* / Q000639:trends; D019295:Computational Biology; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008954:Models, Biological; D014199:Trehalose / Q000378:metabolism*
D000954:Antigens, Surface; D008562:Membrane Glycoproteins; D014199:Trehalose