The protein index ofNostoc commune UTEX 584 (cyanobacteria): changes induced in immobilized cells by water stress

Abstract

Two-dimensional gel electrophoresis was used to analyze the effects of water stress (immobilization and rapid drying, desiccation, rewetting) on the protein index of the desiccation-tolerant cyanobacteriumNostoc commune UTEX 584. Five major “landmark” protein constellations were detected in the protein index of control cells (in liquid culture) and were designated A (1 protein), B (7 proteins), C (8 proteins), D (3 proteins) and E (2 proteins). These included proteins which showed different sensitivities to water stress. Upon immobilization and rapid drying of the cells at a water potential ({ie87-1}) of -99.5 MPa (a_w=0.5) for 30 min, few changes took place in the index. Four conspicuous proteins and the majority of proteins in the size range 18 to 97 K diminished in abundance while most proteins of constellations A, B and C were detected in fluorographs with the same intensity as in the control. Although protein synthesis continued during this time of drying, no novel class of proteins was detected. The level of incorporation of³⁵S in protein increased rapidly during the first 60 min of rehydration, and then decreased gradually for a further 2.5 h. Extant proteins that were hardly detectable after 24 h of drying, reappeared and increased in abundance upon rewetting of cells for 60 min while a number of proteins which disappeared after drying did not appear during this time. No novel class of proteins appeared upon rewetting. During further rehydration, extensive proteolysis was observed.

ThenifH product (Fe protein of nitrogenase) was detected on Western blots — through cross-reaction with antibody — as an acidic polypeptide with a molecular mass of 33.8 K. Fe-protein was detected in immobilized cells after 30 min of drying, in desiccated material, and in rehydrated cells.