The confession of Belhar : a spirituality of reception in the local church

The General Synod of the Dutch Reformed Church took the following decision during October 2011: 'The General Synod decides to make the Confession of Belhar part of its confessional foundation, that is, in terms of its church ordinances, and commission the Moderamen to prepare the necessary processes regarding ecclesiastical law.' This article deals with the perception of, the reception of and resistance against Belhar as confession in a local congregation, Elardus Park. The research also describes how this obstructs the development of missional focus. The main contribution of this article is to argue that the ecumenical concept's full reception should be assessed within the broader framework of building up a missional local church where a spirituality of reception is fully developed in terms of a missional positioning in Africa.L.E.W. (Nederduitse Gereformeerde Kerk Elardus Park) se M-skripsie ‘Die Opbou van ’n Missionale Gemeente en die Resepsie van die Belydenis van Belhar in die NG Gemeente Elarduspark’ is in 2012 voltooi onder leiding van M.N. (Universiteit van Pretoria).http://www.ve.org.zaam201

RNase P: At last, the key finds its lock.:

Apart from the ribosome, the crystal structure of the bacterial RNase P in complex with a tRNA, reported by Reiter and colleagues recently, constitutes the first example of a multiple turnover RNA enzyme. Except in rare exceptions, RNase P is ubiquitous and, like the ribosome, is older than the initial branch point of the phylogenetic tree. Importantly, the structure shows how the RNA and the protein moieties cooperate to process the pre-tRNA substrates. The catalytic site comprises some critical RNA residues spread over the secondary structure but gathered in a compact volume next to the protein, which helps recognize and orient the substrate. The discussion here outlines some important aspects of that crystal structure, some of which could apply to RNA molecules in general

Nucleic Acids Res

We describe a general binding score for predicting the nucleic acid binding probability in proteins. The score is directly derived from physicochemical and evolutionary features and integrates a residue neighboring network approach. Our process achieves stable and high accuracies on both DNA- and RNA-binding proteins and illustrates how the main driving forces for nucleic acid binding are common. Because of the effective integration of the synergetic effects of the network of neighboring residues and the fact that the prediction yields a hierarchical scoring on the protein surface, energy funnels for nucleic acid binding appear on protein surfaces, pointing to the dynamic process occurring in the binding of nucleic acids to proteins

A structural module in RNase P expands the variety of RNA kinks.

RNA structures are built from recurrent modules that can be identified by structural and comparative sequence analysis. In order to assemble sets of helices in compact architectures, modules that introduce bends and kinks are necessary. Among such modules, kink-turns form an important family that presents sequence and structural characteristics. Here, we describe an internal loop in the bacterial type A RNase P RNA that sets helices bound at the junctions exactly in the same relative positions as in kink-turns but without the structural signatures typical of kink-turns. Our work suggests that identifying a structural module in a subset of RNA sequences constitutes a strategy to identify distinct sequential motifs sharing common structural characteristics

Nat Struct Mol Biol

Internal ribosome entry sites (IRESs) facilitate an alternative, end-independent pathway of translation initiation. A particular family of dicistroviral IRESs can assemble elongation-competent 80S ribosomal complexes in the absence of canonical initiation factors and initiator transfer RNA. We present here a cryo-EM reconstruction of a dicistroviral IRES bound to the 80S ribosome. The resolution of the cryo-EM reconstruction, in the subnanometer range, allowed the molecular structure of the complete IRES in its active, ribosome-bound state to be solved. The structure, harboring three pseudoknot-containing domains, each with a specific functional role, shows how defined elements of the IRES emerge from a compactly folded core and interact with the key ribosomal components that form the A, P and E sites, where tRNAs normally bind. Our results exemplify the molecular strategy for recruitment of an IRES and reveal the dynamic features necessary for internal initiation