The enzymatic activity of recombinant Cu-NirK was detected in both cellular fractions (cytoplasmic fraction Selleckchem SBE-β-CD and membranes) and in the culture media. The characterization of the enzyme isolated from the cytoplasmic fraction as well as the culture media revealed important differences in the primary structure of both forms indicating that Hfx. mediterranei could carry out a maturation and exportation process within the cell before the protein is exported to

the S-layer. Several conserved signals found in Cu-NirK from Hfx. mediterranei sequence indicate that these processes are closely related to the Tat system. Furthermore, the N-terminal sequence of the two Cu-NirK subunits constituting different isoforms revealed that translation of this protein could begin at two different points, identifying two possible start codons. The hypothesis proposed in this work for halophilic Cu-NirK processing and exportation LBH589 via the Tat system represents the first approximation of this mechanism in the Halobacteriaceae family and in Prokarya in general. (c) 2013 Elsevier B.V. All rights reserved.”
“Hfq is a bacterial post-transcriptional regulator. It facilitates base-pairing between sRNA

and target mRNA. The mRNA rpoS, which encodes the master regulator us of general stress response, requires Hfq-facilitated base pairing with DsrA small RNA for efficient translation at low temperatures. Two mutually non-exclusive mechanisms have been proposed to explain the process of how Hfq facilitates base pairing of sRNA DsrA to mRNA rpoS: Hfq may form ternary complex with two RNAs

via co-binding to bring the RNA strands into close proximity for optimal annealing; Hfq may bind one or both RNAs, and change its (or their) secondary (or tertiary) structure to facilitate the RNA pairing. Recently, several complex crystal structures of AU(6)A-Hfq-ATP, A(7)-Hfq, and AU(6)A-Hfq-A(7) were acquired, and interesting structural features were extracted from them to deepen our understanding in the RNA binding properties AS1842856 manufacturer of Hfq and its RNA complexes. Furthermore, the formation of ternary complex sRNA-Hfq-mRNA is proved to be necessary for translation activation of rpoS mRNA in vivo. This mini-review summarizes some recent structural biology advances in the research of DsrA-regulated translation of rpoS and the biological implications of the transient ternary complex are discussed.”
“The objective of this paper was to (i) estimate genetic parameters for important physic nut (Jatropha curcas L) traits, and to using these parameters (ii) predict the genetics gains with the selection of superior genotypes using different selection procedures. It was among the objectives of this paper to (iii) compare the efficiency of the different selection methods in order to identify the most suited to be applied in the physic nut breeding program.