The nucleotide sequence of the sulfate and thiosulfate transport gene cluster has been determined and located 3' to the gene (cysP) encoding the thiosulfate-binding protein. Four open reading frames, designated cysT, cysW, cysA, and cysM, have been identified. Similarities in primary structure were observed between (i) the deduced amino acid sequences of CysT and CysW with membrane-bound components of other binding protein-dependent transport systems, (ii) that of the CysA sequence with the "conserved" component of such systems, and (iii) that of the CysM sequence with O-acetylserine sulfhydrylase A (cysK gene product) and the beta-subunit of tryptophan synthase (coded by trpB). Expression of the four genes was analyzed in the T7 promoter-polymerase system.

Both urea and urease were subjects of early scientific investigations. Urea was the first organic molecule to be synthesized and jack bean urease was the first enzyme ever to be crystallized. About 50 years later it was shown to be the first nickel metalloenzyme. Since then, nickel-dependent ureases have been isolated from many bacteria, fungi and higher plants. They have similar structures and mechanisms of catalysis. A urease apoenzyme needs to be activated. This process requires participation of several accessory proteins that incorporate nickel into the urease forming catalytic site. In this review, ureases from various organisms are briefly described and the similarities of their structures discussed. Moreover, the significance of urea recycling in plants is explained and recent literature data about the function and activation of plant ureases are presented.

Two main mechanisms of protein turnover exist in eukaryotic cells: the ubiquitin-proteasome system and the autophagy-lysosomal pathway. Autophagy is an emerging important constituent of many physio...

Sulfur is an essential macronutrient for all living organisms. Plants are able to assimilate inorganic sulfur and incorporate it into organic compounds, while animals rely entirely on organic sources of sulfur. In the last decades sulfate availability in soils has become the major limiting factor for plant production in many countries due to significant reduction of anthropogenic sulfur emission forced by introducing stringent environmental legislation. The sulfur flux after transferring plants from optimal conditions to sulfur deficiency is regulated on multiple levels including transcription, translation and activity of enzymes needed for sulfate assimilation and synthesis of sulfur-containing metabolites. Most of these regulatory steps are not yet fully characterized. Plant responses to sulfur limitation are complex and can be divided into phases depending on the degree of sulfur shortage. The initial responses are limited to adaptations within sulfur metabolic pathway, while multiple metabolic pathways and developmental process are affected when sulfur shortage becomes more severe. The major aim of this work is a comprehensive review of recent progress in understanding the regulation of plant adaptations to sulfur deficit.