Yield and carcass composition of broilers fed with diets based on the concept of crude protein or ideal protein

Two experiments were conducted to evaluate the effect of diets formulated using the criteria of crude protein (CP) and ideal protein (IP) on the yield and carcass composition of male and female broilers. Birds of two broilers strains (Hybro G and Hybro PG) were reared from 1 to 42 days of age during the summer, with average temperatures of 26°C. A completely randomized experimental design was used in a 2 x 2 factorial arrangement, with 6 replicates and 20 birds per pen. On day 42, four birds from each experimental unit were killed and carcass yield and composition were determined. Breast yield was higher in males and females fed the IP-based diet than in birds fed the CP-based diet. Abdominal fat pad and carcass crude protein were statistically similar between the two protein criteria and between strains. Carcass amino acid levels evidenced higher levels of Met, Lys, Met+Cys and Thr in the males fed IP-based diets. No differences were seen between the two criteria for the females. Diets formulated according to IP resulted in better carcass and breast yield, both for males and females

Stepwise self-assembly of a tripeptide from molecular dimers to supramolecular beta-sheets in crystals and amyloid-like fibrils in the solid state

The terminally protected tripeptide Boc-Ala(1)-Leu(2)-Ala(3)-OMe 1 forms antiparallel hydrogen-bonded dimers of two different conformers in the asymmetric unit and the individual dimers then self-associate to form supramolecular beta-sheet structures in crystals and amyloid-like fibrils in the solid state

Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase

The vaccinia virus mRNA capping enzyme is a multifunctional heterodimeric protein associated with the viral polymerase that both catalyses the three steps of mRNA capping and regulates gene transcription. The structure of a subcomplex comprising the C-terminal N7-methyl-transferase (MT) domain of the large D1 subunit, the stimulatory D12 subunit and bound S-adenosyl-homocysteine (AdoHcy) has been determined at 2.7 Å resolution and reveals several novel features of the poxvirus capping enzyme. The structure shows for the first time the critical role played by the proteolytically sensitive N-terminus of the MT domain in binding the methyl donor and in catalysis. In addition, the poxvirus enzyme has a completely unique mode of binding of the adenosine moiety of AdoHcy, a feature that could be exploited for design of specific anti-poxviral compounds. The structure of the poxvirus-specific D12 subunit suggests that it was originally an RNA cap 2′O-MT that has evolved to a catalytically inactive form that has been retained for D1 stabilisation and MT activity enhancement through an allosteric mechanism

Polycomb Protein SCML2 Regulates the Cell Cycle by Binding and Modulating CDK/CYCLIN/p21 Complexes

Polycomb group (PcG) proteins are transcriptional repressors of genes involved in development and differentiation, and also maintain repression of key genes involved in the cell cycle, indirectly regulating cell proliferation. The human SCML2 gene, a mammalian homologue of the Drosophila PcG protein SCM, encodes two protein isoforms: SCML2A that is bound to chromatin and SCML2B that is predominantly nucleoplasmic. Here, we purified SCML2B and found that it forms a stable complex with CDK/CYCLIN/p21 and p27, enhancing the inhibitory effect of p21/p27. SCML2B participates in the G1/S checkpoint by stabilizing p21 and favoring its interaction with CDK2/CYCE, resulting in decreased kinase activity and inhibited progression through G1. In turn, CDK/CYCLIN complexes phosphorylate SCML2, and the interaction of SCML2B with CDK2 is regulated through the cell cycle. These findings highlight a direct crosstalk between the Polycomb system of cellular memory and the cell-cycle machinery in mammals