The selectivity and specificity of autophagy in drosophila

Autophagy is a process of cellular self-degradation and is a major pathway for elimination of cytoplasmic material by the lysosomes. Autophagy is responsible for the degradation of damaged organelles and protein aggregates and therefore plays a significant role in cellular homeostasis. Despite the initial belief that autophagy is a nonselective bulk process, there is growing evidence during the last years that sequestration and degradation of cellular material by autophagy can be accomplished in a selective and specific manner. Given the role of autophagy and selective autophagy in several disease related processes such as tumorigenesis, neurodegeneration and infections, it is very important to dissect the molecular mechanisms of selective autophagy, in the context of the system and the organism. An excellent genetically tractable model organism to study autophagy is Drosophila, which appears to have a highly conserved autophagic machinery compared with mammals. However, the mechanisms of selective autophagy in Drosophila have been largely unexplored. The aim of this review is to summarize recent discoveries about the selectivity of autophagy in Drosophila

Hepatitis Delta Virus RNA Replication

Hepatitis delta virus (HDV) is a distant relative of plant viroids in the animal world. Similar to plant viroids, HDV replicates its circular RNA genome using a double rolling-circle mechanism. Nevertheless, the production of hepatitis delta antigen (HDAg), which is indispensible for HDV replication, is a unique feature distinct from plant viroids, which do not encode any protein. Here the HDV RNA replication cycle is reviewed, with emphasis on the function of HDAg in modulating RNA replication and the nature of the enzyme involved

BILAN DES DECLARATIONS DE MALADIES PROFESSIONNELLES N 97 ET N 98 CONCERNANT LES AFFECTIONS CHRONIQUES DU RACHIS LOMBAIRE TRANSMISES A L'INSPECTION MEDICALE REGIONALE DU NORD PAS-DE-CALAIS EN 1999

LILLE2-BU Santé-Recherche (593502101) / SudocPARIS-BIUM (751062103) / SudocSudocFranceF

The Cell Wall Peptidoglycan of Bacillus megaterium KM. I. Studies on the Stereochemistry of α,α'-Diaminopimelic Acid

α,α'-Diaminopimelic acid (DAP) occurs in the wall peptidoglycan of Bacillus megaterium KM predominantly in the form of its meso isomer (about 85% of the total residues) and, in minor amounts, in the form of its DD isomer. The amino groups on the L carbon of the meso-DAP residues are involved in peptide linkages to the glutamic acid residues. Most of the amino groups on the D carbon of the meso-DAP residues are free; some of them are substituted, thus probably serving to cross-link peptide subunits. These amino groups can be liberated by a Streptomyces endopeptidase. None of the DD-DAP residues have amino groups free. Moreover, these groups are not liberated by endopeptidase treatment. The peptidoglycan upon enzymatic degradation yields mainly two fractions. A major fraction is composed of disaccharide peptide monomer subunits containing only the meso isomer of DAP. A second minor fraction is composed of disaccharide peptide oligomers containing both meso and DD isomers of DAP. The meso-DAP residues isolated as monodinitrophenyl derivatives from both fractions have optical rotations and optical rotatory dispersions identical with that of synthetic monodinitrophenyl-meso-DAP obtained by dinitrophenylation of the amino group on the D carbon. The assignment of the DD configuration to the DAP residues which are not meso rests upon the optical rotatory properties of their bisdinitrophenyl derivatives