title: Distribution and partial characterization of seasonally expressed proteins in different aged shoots and roots of 'Loring' peach (Prunus persica).
abstract: During autumnal leaf senescence, leaf nitrogen in deciduous trees is translocated to storage sites, especially bark and xylem tissues. Proteins that accumulate in large amounts in bark and xylem in winter and are absent from these organs in summer are called storage proteins, and are believed to be vehicles for storing nitrogen reserves. These reserves are important for spring growth and help trees tolerate or recover from both abiotic and biotic stresses. Based on seasonal patterns of accumulation, we previously identified three storage proteins with molecular masses of 60, 19 and 16 kDa in bark tissues of 'Loring' peach (Prunus persica (L.) Batsch). To characterize the distribution of these proteins in different-aged tissues and to determine if they have any function other than nitrogen storage, we examined their seasonal distribution in bark tissues of current-year and 1-year-old shoots, scaffold branches, main trunks and 4-5-year-old roots of 'Loring' peach. Verification of protein identity was based on molecular mass and reactions with antibodies directed against each specific protein. Protein distribution was variable. For all three proteins, the greatest amount was present in mid-winter in current-year and 1-year-old shoots. These tissues also showed the greatest seasonal variation in the amount of protein present. The 16 kDa protein was present only in the youngest shoots, whereas the 19 kDa protein was present in all tissues examined. The 60 kDa protein was absent in root tissue. The amino acid composition and sequence of each protein were determined. The 60 kDa protein was identified as a dehydrin, and the 19 kDa protein appeared to be related to a family of allergen proteins in Rosaceous plants, some members of which are associated with pathogenesis-related proteins. The amino acid sequence of the 16 kDa protein appeared to have no homology with any proteins in the SwissProt database. Therefore, it is likely that the 16 kDa protein, in a strict sense, is a bark storage protein. Defining storage proteins solely by their pattern of accumulation and the extent to which they accumulate may not be a good functional definition. It is possible that storage proteins have functional roles in addition to nitrogen storage.
authors.affiliation: United States Department of Agriculture-Agricultural Research Service, 2217 Wiltshire Road, Kearneysville, WV 25430, USA. mwisniew@afrs.ars.usda.gov
authors.forename: Michael
authors.initials: M
authors.lastname: Wisniewski
authors.forename: Carole
authors.initials: C
authors.lastname: Bassett
authors.forename: Rajeev
authors.initials: R
authors.lastname: Arora
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel; D018506:Gene Expression Regulation, Plant / Q000502:physiology; D015151:Immunoblotting; D024301:Plant Bark / Q000378:metabolism / Q000502:physiology; D010940:Plant Proteins / Q000096:biosynthesis; D018517:Plant Roots / Q000378:metabolism / Q000502:physiology*; D018520:Plant Shoots / Q000378:metabolism / Q000502:physiology*; D027861:Prunus / Q000378:metabolism / Q000502:physiology*; D012621:Seasons; D014197:Trees / Q000378:metabolism / Q000502:physiology*
chemical_list: D010940:Plant Proteins