PubMed HealthSearch

Biomedical subjects

W Bottke

Publications and source records attributed to W Bottke.

2 recordsLinked to original sources

Chromosome-associated paracrystalline nuclear inclusions in the spermatocytes of a pulmonate snail, Planorbarius corneus L.

Chromosome-associated paracrystalloids are regularly found in the spermatocytes of snails which were reared in the laboratory. They seem to be largely specific for the male gametocytes as they have been observed only in few cases in the oocytes. It is likely that paracrystalloids are formed during pachytene at the site of large heterochromatic knobs which originate by fusion of heterochromatic terminal segments of some bivalents. During diplotene they are always connected with the telomeres of three or four bivalents, thus forming a large trefoil-like structure. During metaphase I paracrystalloids are shed off from the chromosomes and transferred to the cytoplasm. In early spermatids they are found again in the nuclei, where they "fade away" during spermiogenesis. Histochemically they consist of basic proteins, which are probably crystallized in the cubic system. Radioactive labeling of the structure could not be achieved, neither by 3H-uridine or thymidine, nor by amino acids. The functional significance of this peculiar structure in unknown. Certain features justify a comparison with synaptonemal polycomplexes.

Animals

Structure, function, and evolution of ferritins.

The ferritins of animals and plants and the bacterioferritins (BFRs) have a common iron-storage function in spite of differences in cytological location and biosynthetic regulation. The plant ferritins and BFRs are more similar to the H chains of mammals than to mammalian L chains, with respect to primary structure and conservation of ferroxidase center residues. Hence they probably arose from a common H-type ancestor. The recent discovery in E. coli of a second type of iron-storage protein (FTN) resembling ferritin H chains raises the question of what the relative roles of these two proteins are in this organism. Mammalian L ferritins lack ferroxidase centers and form a distinct group. Comparison of the three-dimensional structures of mammalian and invertebrate ferritins, as well as computer modeling of plant ferritins and of BFR, indicate a well conserved molecular framework. The characterisation of numerous ferritin homopolymer variants has allowed the identification of some of the residues involved in iron uptake and an investigation of some of the functional differences between mammalian H and L chains.

Amino Acid Sequence