Behavioral Competencies and Learning Methods for IT Project Management: An Exploratory Study

What do IT project managers consider to be the critical skills necessary for project success, and how have they developed those skills? The aim of this research has been to answer these questions. We interviewed 23 experienced IT project managers from 11 organizations, focusing first on what the managers perceived as their most critical project management skills, and then on how they had developed those skills. We also discussed their exposure to a wide variety of organizational development interventions. By focusing on how project managers actually learned critical skills, we have been able to uncover the importance of informal learning channels, often involving project experiences, for the development of IT project management skills

PROJECT MANAGER COMPETENCIES AND PERFORMANCE OUTCOMES IN IT PROJECTS

Meeting performance targets for IT projects is difficult, and skilled project managers have been identified as a key factor in maximizing the possibilities of success. Our goal in this study was to identify critical behavioural competencies for IT project managers, including competencies necessary for entry-level positions and competencies that distinguish superior performance in IT project management. Two categories of competence, team leadership and concern for order, were associated with higher levels of IT project performance outcomes. The behaviours within these two categories provide a useful focus for organizations seeking to improve their project management performance. Some of these behaviours - for example, detailed planning and managing meetings - are entry-level behaviours that should be the target of basic training for novice project managers. Other behaviours - for example, accurate estimation and problem solving strategies - were observed in fewer respondents and could be the focus of more advanced training for incumbent project managers. Additionally, two valuable but infrequently observed behaviours ? creating a compelling vision and ensuring alignment with business strategic goals ? were correlated with performance related to supporting longer term business benefits from IT projects, suggesting that developing project manager competence in these behaviours would be particularly beneficial for achieving long-term success from IT projects

Probing regulon of ArcA in Shewanella oneidensis MR-1 by integrated genomic analyses

<p>Abstract</p> <p>Background</p> <p>The Arc two-component system is a global regulator controlling many genes involved in aerobic/anaerobic respiration and fermentative metabolism in <it>Escherichia coli</it>. <it>Shewanella oneidensis </it>MR-1 contains a gene encoding a putative ArcA homolog with ~81% amino acid sequence identity to the <it>E. coli </it>ArcA protein but not a full-length <it>arcB </it>gene.</p> <p>Results</p> <p>To understand the role of ArcA in <it>S. oneidensis</it>, an <it>arcA </it>deletion strain was constructed and subjected to both physiological characterization and microarray analysis. Compared to the wild-type MR-1, the mutant exhibited impaired aerobic growth and a defect in utilizing DMSO in the absence of O₂. Microarray analyses on cells grown aerobically and anaerobically on fumarate revealed that expression of 1009 genes was significantly affected (<it>p </it>< 0.05) by the mutation. In contrast to <it>E. coli </it>ArcA, the protein appears to be dispensable in regulation of the TCA cycle in <it>S. oneidensis</it>. To further determine genes regulated by the Arc system, an ArcA recognition weight matrix from DNA-binding data and bioinformatics analysis was generated and used to produce an ArcA sequence affinity map. By combining both techniques, we identified an ArcA regulon of at least 50 operons, of which only 6 were found to be directly controlled by ArcA in <it>E. coli</it>.</p> <p>Conclusion</p> <p>These results indicate that the Arc system in <it>S. oneidensis </it>differs from that in <it>E. coli </it>substantially in terms of its physiological function and regulon while their binding motif are strikingly similar.</p

Suffizienz als Business Case

Über Suffizienz wird bisher ausschließlich als Orientierungsmuster für individuellen Konsum diskutiert. Der folgende Beitrag zeigt, dass die Debatte über Suffizienz durchaus Geschäftschancen für Unternehmen eröffnet

Slow Protein Dynamics Elicits New Enzymatic Functions by Means of Epistatic Interactions

Protein evolution depends on the adaptation of these molecules to different functional challenges. This occurs by tuning their biochemical, biophysical, and structural traits through the accumulation of mutations. While the role of protein dynamics in biochemistry is well recognized, there are limited examples providing experimental evidence of the optimization of protein dynamics during evolution. Here we report an NMR study of four variants of the CTX-M β-lactamases, in which the interplay of two mutations outside the active site enhances the activity against a cephalosporin substrate, ceftazidime. The crystal structures of these enzymes do not account for this activity enhancement. By using NMR, here we show that the combination of these two mutations increases the backbone dynamics in a slow timescale and the exposure to the solvent of an otherwise buried β-sheet. The two mutations located in this β-sheet trigger conformational changes in loops located at the opposite side of the active site. We postulate that the most active variant explores alternative conformations that enable binding of the more challenging substrate ceftazidime. The impact of the mutations in the dynamics is context-dependent, in line with the epistatic effect observed in the catalytic activity of the different variants. These results reveal the existence of a dynamic network in CTX-M β-lactamases that has been exploited in evolution to provide a net gain-of-function, highlighting the role of alternative conformations in protein evolution.Fil: Rossi, María Agustina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Palzkill, Timothy. Baylor College Of Medicine (baylor College Of Medicine);Fil: Almeida, Fabio C L. Universidade Federal do Rio de Janeiro; BrasilFil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentin

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Einführung in das Schwerpunktthem

Structural basis for different substrate profiles of two closely related class D β-lactamases and their inhibition by halogens

OXA-163 and OXA-48 are closely related class D β-lactamases that exhibit different substrate profiles. OXA-163 hydrolyzes oxyimino-cephalosporins, particularly ceftazidime, while OXA-48 prefers carbapenem substrates. OXA-163 differs from OXA-48 by one substitution (S212D) in the active-site β5 strand and a four-amino acid deletion (214-RIEP-217) in the loop connecting the β5 and β6 strands. Although the structure of OXA-48 has been determined, the structure of OXA-163 is unknown. To further understand the basis for their different substrate specificities, we performed enzyme kinetic analysis, inhibition assays, X-ray crystallography, and molecular modeling. The results confirm the carbapenemase nature of OXA-48 and the ability of OXA-163 to hydrolyze the oxyimino-cephalosporin ceftazidime. The crystal structure of OXA-163 determined at 1.72 Å resolution reveals an expanded active site compared to that of OXA-48, which allows the bulky substrate ceftazidime to be accommodated. The structural differences with OXA-48, which cannot hydrolyze ceftazidime, provide a rationale for the change in substrate specificity between the enzymes. OXA-163 also crystallized under another condition that included iodide. The crystal structure determined at 2.87 Å resolution revealed iodide in the active site accompanied by several significant conformational changes, including a distortion of the β5 strand, decarboxylation of Lys73, and distortion of the substrate-binding site. Further studies showed that both OXA-163 and OXA-48 are inhibited in the presence of iodide. In addition, OXA-10, which is not a member of the OXA-48-like family, is also inhibited by iodide. These findings provide a molecular basis for the hydrolysis of ceftazidime by OXA-163 and, more broadly, show how minor sequence changes can profoundly alter the active-site configuration and thereby affect the substrate profile of an enzyme