Analysis of the admissions tests for teacher training in Spain and Finland: knowledge or competences

One of the most decisive factors in the quality of education and academic performance of students is quality, preparation and dedication of the teachers. The exquisite system of selecting candidates for teacher training programs is one of the fundamentals of success of the Finnish Education System. The responsibility of choosing the best students to convert them into teachers is a challenge that involves a significant reform of university admission. Achieving this goal involves the choice of strategies and educational tools in accordance to the complexity of the demands presented by the teaching profession in the digital age. This study describes, analyzes and compares the admission tests in the University of Spain (PAU) and Finland (VAKAVA), for those who wish to become professional educators, in order to understand the possible influence of these tests to select the most suitable candidates to develop into future teaching professionals. The results showed that in Spain, the entrance test to universities is developed in a general way for all the students that aspire to any field of knowledge, while in Finland, the test is specific and particular for students aspiring to the field of education. The results of this study can guide and encourage the necessary changes that have to be done in the admission tests to Spanish university in general and to teacher education faculties in particular.

ADP-Ribose-1"-Monophosphatase: a Conserved Coronavirus Enzyme That Is Dispensable for Viral Replication in Tissue Culture

Replication of the ~30-kb plus-strand RNA genome of coronaviruses and synthesis of an extensive set of subgenome-length RNAs are mediated by the replicase-transcriptase, a membrane-bound protein complex containing several cellular proteins and up to 16 viral nonstructural proteins (nsps) with multiple enzymatic activities, including protease, polymerase, helicase, methyltransferase, and RNase activities. To get further insight into the replicase gene-encoded functions, we characterized the coronavirus X domain, which is part of nsp3 and has been predicted to be an ADP-ribose-1"-monophosphate (Appr-1"-p) processing enzyme. Bacterially expressed forms of human coronavirus 229E (HCoV-229E) and severe acute respiratory syndrome-coronavirus X domains were shown to dephosphorylate Appr-1"-p, a side product of cellular tRNA splicing, to ADP-ribose in a highly specific manner. The enzyme had no detectable activity on several other nucleoside phosphates. Guided by the crystal structure of AF1521, an X domain homolog from Archaeoglobus fulgidus, potential active-site residues of the HCoV-229E X domain were targeted by site-directed mutagenesis. The data suggest that the HCoV-229E replicase polyprotein residues, Asn 1302, Asn 1305, His 1310, Gly 1312, and Gly 1313, are part of the enzyme's active site. Characterization of an Appr-1"-pase-deficient HCoV-229E mutant revealed no significant effects on viral RNA synthesis and virus titer, and no reversion to the wild-type sequence was observed when the mutant virus was passaged in cell culture. The apparent dispensability of the conserved X domain activity in vitro indicates that coronavirus replicase polyproteins have evolved to include nonessential functions. The biological significance of the novel enzymatic activity in vivo remains to be investigated.