Nuclear crystalloids in sieve elements of Boraginaceae: a protein digestion study.

Nuclear crystalloids have been found in sieve elements of several Boraginaceae. Nuclei of differentiating sieve elements of Echium and other genera except Amsinckia contain one or more crystalloids composed of thin rods densely packed in parallel arrangement. After the nuclei disintegrate in the maturing sieve element the crystalloids are released into the cell lumen where they persist intact. In Amsinckia the crystalloid consists of two components: a dense component, similar to the crystalloid in the other genera and a loosely arranged paracrystalline component. The proteinaceous nature of the nuclear crystalloids and their possible similarity to P-protein was investigated by enzyme digestion techniques. Three proteolytic enzymes were employed in this study: protease, pepsin and trypsin. Successful digestion of the dense crystalloid in both Echium and Amsinckia was obtained with each enzyme tested. P-protein plugging the sieve plate pores was also digested. The loose component in Amsinckia and the aggregated and dispersed P-protein were not affected by the enzyme digestion procedures. These results seemed to indicate that the density or compactness of the proteinaceous inclusions may play a role in the differential response.