Fic and non-Fic AMPylases: protein AMPylation in metazoans

Protein AMPylation refers to the covalent attachment of an AMP moiety to the amino acid side chains of target proteins using ATP as nucleotide donor. This process is catalysed by dedicated AMP transferases, called AMPylases. Since this initial discovery, several research groups have identified AMPylation as a critical post-translational modification relevant to normal and pathological cell signalling in both bacteria and metazoans. Bacterial AMPylases are abundant enzymes that either regulate the function of endogenous bacterial proteins or are translocated into host cells to hijack host cell signalling processes. By contrast, only two classes of metazoan AMPylases have been identified so far: enzymes containing a conserved filamentation induced by cAMP (Fic) domain (Fic AMPylases), which primarily modify the ER-resident chaperone BiP, and SelO, a mitochondrial AMPylase involved in redox signalling. In this review, we compare and contrast bacterial and metazoan Fic and non-Fic AMPylases, and summarize recent technological and conceptual developments in the emerging field of AMPylation.     

pi-Turns: types,systematics and the context of their occurrence in protein structures

Background  

For a proper understanding of protein structure and folding it is important to know if a polypeptide segment adopts a conformation inherent in the sequence or it depends on the context of its flanking secondary structures. Turns of various lengths have been studied and characterized starting from three-residue γ-turn to six-residue π-turn. The Schellman motif occurring at the C-terminal end of α-helices is a classical example of hydrogen bonded π-turn involving residues at (i) and (i+5) positions. Hydrogen bonded and non-hydrogen bonded β- and α-turns have been identified previously; likewise, a systematic characterization of π-turns would provide valuable insight into turn structures.     

Effect of fermentation ensilaging on recovery of oil from fresh water fish viscera

Fish viscera are an important source for biomolecules such as protein and lipids. Studies were carried out to assess fermentation ensilaging as a method for recovery of oil from fresh water fish viscera. The total lipid content in the viscera ranged from 19% to 21% and upto 85% of this could be recovered by fermentation. Fermentation using added lactic cultures (Enterococcus faecium HAB01 and Pediococcus acidilactici K7) did not show any advantage over natural fermentation with respect to recovery of oil and no differences were observed in fatty acid composition of oil recovered by fermentation using different cultures. Activity of acidic, neutral and alkaline proteases decreased during fermentation. Eventhough degree of protein hydrolysis increased during fermentation with highest (62.3%) being in fermentation using Pediococcus acidilactici K7 no differences were found in oil recovery. With decrease in protease activity the rate of change in degree of hydrolysis also decreased.