Lessons learned from the implementation of a Management Information System designed at the University of Otavalo, Ecuador / Lecciones aprendidas de la implementación de un Sistema de Información Gerencial diseñado en la Universidad de Otavalo, Ecuador

Abstract The purpose of this paper is to analyze the essential features of a Management Information System (MIS), designed and implemented at the Universidad de Otavalo to support strategic planning, institutional evaluation, and decision making. A five-phase and fifteen-stage process was applied, along with their corresponding techniques and expected results. Based on the literature review and their experience with the implementation, the authors devised a novel MIS implementation approach, comprising the following phases: planning, information analysis, MIS design, implementation and evaluation. The MIS consisted of four main modules: teaching, research, linkages with society, and management, and was based on the client-server model. The literature review did not yield any publications that discussed truly integrated management information systems applied to university management covering the four main modules, thus confirming the originality of the work described in this paper. The MIS implementation results contributed to the improvement of the management of the university through the automation of most of the processes and activities related to institutional planning and evaluation, and considerably accelerated the processing and analysis of useful information for decision making.

Resumen El objetivo de este estudio fue analizar las características esenciales de un Sistema de Información Gerencial (SIG), diseñado e implementado en la Universidad de Otavalo para apoyar la planificación estratégica, la evaluación institucional y la toma de decisiones. Se aplicó un procedimiento integrado por cinco fases y quince etapas, con sus correspondientes técnicas y resultados esperados. En base a la revisión bibliográfica y las experiencias devenidas de la implementación, los autores elaboraron un procedimiento original, cuyas fases son: Planificación, Análisis de la información, Diseño del SIG, Implementación y Evaluación. El SIG estuvo formado por cuatro módulos principales: academia, investigación vinculación y administración, y se basó en el modelo cliente-servidor. En la búsqueda realizada no se encontraron evidencias de publicaciones referidas a sistemas integrados aplicados a la gestión universitaria, considerando el contenido de los cuatro módulos señalados, lo cual fundamenta la originalidad del trabajo. Los resultados de la implementación del SIG contribuyeron al perfeccionamiento de la gestión universitaria, mediante la automatización de la mayoría de los procesos y actividades vinculados con la planificación y la evaluación institucional y agilizaron considerablemente el procesamiento y análisis de la información útil para la toma de decisiones.

Role of transmembrane domain 8 in substrate selectivity and translocation of SteT, a member of the L-amino acid transporter (LAT) family.

System l-amino acid transporters (LAT) belong to the amino acid, polyamine, and organic cation superfamily of transporters and include the light subunits of heteromeric amino acid transporters and prokaryotic homologues. Cysteine reactivity of SteT (serine/threonine antiporter) has been used here to study the substrate-binding site of LAT transporters. Residue Cys-291, in transmembrane domain 8 (TM8), is inactivated by thiol reagents in a substrate protectable manner. Surprisingly, DTT activated the transporter by reducing residue Cys-291. Cysteine-scanning mutagenesis of TM8 showed DTT activation in the single-cysteine mutants S287C, G294C, and S298C, lining the same alpha-helical face. S-Thiolation in Escherichia coli cells resulted in complete inactivation of the single-cysteine mutant G294C. l-Serine blocked DTT activation with an EC(50) similar to the apparent K(M) of this mutant. Thus, S-thiolation abolished substrate translocation but not substrate binding. Mutation of Lys-295, to Cys (K295C) broadened the profile of inhibitors and the spectrum of substrates with the exception of imino acids. A structural model of SteT based on the structural homologue AdiC (arginine/agmatine antiporter) positions residues Cys-291 and Lys-295 in the putative substrate binding pocket. All this suggests that Lys-295 is a main determinant in the recognition of the side chain of SteT substrates. In contrast, Gly-294 is not facing the surface, suggesting conformational changes involving TM8 during the transport cycle. Our results suggest that TM8 sculpts the substrate-binding site and undergoes conformational changes during the transport cycle of SteT.

Functional and structural characterization of the first prokaryotic member of the L-amino acid transporter (LAT) family: a model for APC transporters.

We have identified YkbA from Bacillus subtilis as a novel member of the L-amino acid transporter (LAT) family of amino acid transporters. The protein is approximately 30% identical in amino acid sequence to the light subunits of human heteromeric amino acid transporters. Purified His-tagged YkbA from Escherichia coli membranes reconstituted in proteoliposomes exhibited sodium-independent, obligatory exchange activity for L-serine and L-threonine and also for aromatic amino acids, albeit with less activity. Thus, we propose that YkbA be renamed SteT (Ser/Thr exchanger transporter). Kinetic analysis supports a sequential mechanism of exchange for SteT. Freeze-fracture analysis of purified, functionally active SteT in proteoliposomes, together with blue native polyacrylamide gel electrophoresis and transmission electron microscopy of detergent-solubilized purified SteT, suggest that the transporter exists in a monomeric form. Freeze-fracture analysis showed spherical particles with a diameter of 7.4 nm. Transmission electron microscopy revealed elliptical particles (diameters 6 x 7 nm) with a distinct central depression. To our knowledge, this is the first functional characterization of a prokaryotic member of the LAT family and the first structural data on an APC (amino acids, polyamines, and choline for organocations) transporter. SteT represents an excellent model to study the molecular architecture of the light subunits of heteromeric amino acid transporters and other APC transporters.