Individual Readiness for Change in the Context of Enterprise Resource Planning Systems Implementation

The present study takes a bottom-up approach and investigates the organizational implications of ERP systems implementation in organizations. We adopt a likely point of view of employees and study the ERP integration process along 3 dimensions: people, processes, and information. In this manner we discover the ERP-specific sources of resistance that could affect negatively the deployment of the software. Then, we argue that a general set of beliefs shapes employees readiness to change to ERP use and provides the foundation for resistance or for adoptive behavior. We define the concept of readiness for change in the context of ERP and introduce a readiness for change assessment approach. Then, we test empirically the study hypotheses upon which the research model was build. The results obtained offer insights into factors that can improve the effectiveness of ERP implementation strategies and underline the importance of change management for the success of such projects

Yeast Upf1 CH domain interacts with Rps26 of the 40S ribosomal subunit

The central nonsense-mediated mRNA decay (NMD) regulator, Upf1, selectively targets nonsense-containing mRNAs for rapid degradation. In yeast, Upf1 preferentially associates with mRNAs that are NMD substrates, but the mechanism of its selective retention on these mRNAs has yet to be elucidated. Previously, we demonstrated that Upf1 associates with 40S ribosomal subunits. Here, we define more precisely the nature of this association using conventional and affinity-based purification of ribosomal subunits, and a two-hybrid screen to identify Upf1-interacting ribosomal proteins. Upf1 coimmunoprecipitates specifically with epitope-tagged 40S ribosomal subunits, and Upf1 association with high-salt washed or puromycin-released 40S subunits was found to occur without simultaneous eRF1, eRF3, Upf2, or Upf3 association. Two-hybrid analyses and in vitro binding assays identified a specific interaction between Upf1 and Rps26. Using mutations in domains of UPF1 known to be crucial for its function, we found that Upf1:40S association is modulated by ATP, and Upf1:Rps26 interaction is dependent on the N-terminal Upf1 CH domain. The specific association of Upf1 with the 40S subunit is consistent with the notion that this RNA helicase not only triggers rapid decay of nonsense-containing mRNAs, but may also have an important role in dissociation of the premature termination complex