The effects of salt on the pattern of protein synthesis in barley roots

• Published in: Plant physiology (Bethesda) 1987-03, Vol.83 (3), p.517-524
• Main Authors: Hurkman, W.J, Tanaka, C.K
• Format: Article
• Language: English
• Subjects: Agronomy. Soil science and plant productions; Antibodies; Barley; Biological and medical sciences; CHLORURE DE SODIUM; CLORURO DE SODIO; Deficiencies. Phytotoxicity of elements. Salinity; Electrophoresis; Environmental and Stress Physiology; ETIQUETADO; Fundamental and applied biological sciences. Psychology; Gels; General agronomy. Plant production; HORDEUM VULGARE; LABELLING; MARQUAGE; Messenger RNA; Nutrient solutions; Plant physiology and development; Plant roots; Plants; PROTEIN SYNTHESIS; PROTEINAS; PROTEINE; PROTEINS; RACINE; RAICES; ROOTS; SINTESIS DE PROTEINAS; SODIUM CHLORIDE; Soil-plant relationships. Soil fertility. Fertilization. Amendments; STRESS; SYNTHESE PROTEIQUE; Table salt; Water and solutes. Absorption, translocation and permeability
• ISSN: 0032-0889; 1532-2548
• DOI: 10.1104/pp.83.3.517

The effect of salt stress on the incorporation of [35S]methionine into protein was examined in roots of barley (Hordeum vulgare L. cv California Mariout 72). Plants were grown in nutrient solution with or without 200 millimolar NaCl. Roots of intact plants were labeled in vivo and proteins were extracted and analyzed by fluorography of two-dimensional gels. Although the protein patterns for control and salt-stressed plants were qualitatively similar, the net synthesis of a number of proteins was quantitatively changed. The most striking change was a significant increase of label in two protein pairs that had pIs of approximately 6.3 and 6.5. Each pair consisted of proteins of approximately 26 and 27 kilodaltons (kD). In roots of control plants, the 27-kD proteins were more heavily labeled in the microsomal fraction relative to the 26-kD proteins, whereas the 26-kD proteins were enriched in the post 178,000 g supernatant fraction; in roots of salt treated plants, the 26- and 27-kD proteins were more intensely labeled in both fractions. Labeling of the 26- and 27-kD proteins returned to control levels when salt-stressed plants were transferred to nutrient solution without NaCl. No cross-reaction was detected between the antibody to the 26-kD protein from salt-adapted tobacco cells and the 26- and 27-kD proteins of barley.