title: Dehydration-regulated processing of late embryogenesis abundant protein in a desiccation-tolerant nematode.
abstract: Late embryogenesis abundant (LEA) proteins occur in desiccation-tolerant organisms, including the nematode Aphelenchus avenae, and are thought to protect other proteins from aggregation. Surprisingly, expression of the LEA protein AavLEA1 in A. avenae is partially discordant with that of its gene: protein is present in hydrated animals despite low cognate mRNA levels. Moreover, on desiccation, when its gene is upregulated, AavLEA1 is specifically cleaved to discrete, smaller polypeptides. A processing activity was found in protein extracts of dehydrated, but not hydrated, nematodes, and main cleavage sites were mapped to 11-mer repeated motifs in the AavLEA1 sequence. Processed polypeptides retain function as protein anti-aggregants and we hypothesise that the expression pattern and cleavage of LEA protein allow rapid, maximal availability of active molecules to the dehydrating animal.
authors: Institute of Biotechnology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QT, UK.
authors: Kshamata
authors: K
authors: Goyal
authors: Claudia
authors: C
authors: Pinelli
authors: Sarah L
authors: SL
authors: Maslen
authors: Rakesh K
authors: RK
authors: Rastogi
authors: Elaine
authors: E
authors: Stephens
authors: Alan
authors: A
authors: Tunnacliffe
mesh_terms: D000222:Adaptation, Physiological; D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D003890:Desiccation; D004591:Electrophoresis, Polyacrylamide Gel; D015801:Helminth Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009348:Nematoda / Q000196:embryology* / Q000502:physiology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D015801:Helminth Proteins