Resolving agency issues in client-contractor relationships to deliver project success

In our research we seek to explain why some relationships between project client and contractors are managed in such a way that leads to success and others are not. In doing so, we analyze how the relational risk that exists when a client sources a project from an external organization is managed. We view the topic through a lens of agency theory and we use a multiple case study research design, analyzing projects from the construction and clinical research business sectors that had varying degrees of success. We extend knowledge of managing relational risk by developing a framework for resolving agency-related issues to deliver project success. The framework encompasses mechanisms to managing relational risk which we classify in five broad areas: contract, understanding, resources, education and delegation – the CURED framework. These areas reflect both formal and informal mechanisms as described in existing literature

Conditions of Success for Earned Value Analysis in Projects

Earned Value Analysis (EVA) is a method that has gained traction in some business sectors to report project progress and help control performance. Yet the literature reports mixed results as to its effectiveness in helping deliver successful projects and, additionally, much of the previous studies on the topic is conceptual in nature focusing on the design of the EVA system. We therefore extend knowledge on EVA by analysing the impact of EVA on the levels of success of two projects that utilised the method. This is done through the prism of agency and organisational justice theories. A framework is proposed of EVA conditions of success, incorporating both design and operational aspects of the EVA system. The framework is used to develop testable propositions that can guide further research into the effects of EVA-based systems on the creation of agency-related characteristics in the project environment that are conducive to project success

Corrosion inhibition capacity of two heterocyclic oximes on copper in nitric acid: electrochemical, quantum chemical and surface morphological investigations

Two heterocyclic oximes (E)-N-hydroxy-1-(pyridin-2-yl)methanimine (Hp2ylm) and (E)-N-hydroxy-1-(pyridin-3-yl)methanimine (Hp3ylm) were synthesized from pyridine-2-carbaldehyde and pyridine-3-carbaldehyde, respectively. These oximes were characterized by various spectroscopic tools like UV, IR, MASS and NMR. The inhibition capacity of these oximes against copper corrosion in 0.1 M HNO3 was determined by polarization and impedance spectroscopic studies (EIS). At all concentrations, Hp3ylm exhibited higher inhibition efficiency than Hp2ylm. Attempt was made to illustrate the mechanism of corrosion inhibition by these oximes with the help of adsorption isotherm, scanning electron microscopic (SEM) and quantum chemical studies

The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons

Stalled ribosomes at the endoplasmic reticulum (ER) are covalently modified with the ubiquitin-like protein UFM1 on the 60S ribosomal subunit protein RPL26 (also known as uL24) 1,2. This modification, which is known as UFMylation, is orchestrated by the UFM1 ribosome E3 ligase (UREL) complex, comprising UFL1, UFBP1 and CDK5RAP3 (ref. 3). However, the catalytic mechanism of UREL and the functional consequences of UFMylation are unclear. Here we present cryo-electron microscopy structures of UREL bound to 60S ribosomes, revealing the basis of its substrate specificity. UREL wraps around the 60S subunit to form a C-shaped clamp architecture that blocks the tRNA-binding sites at one end, and the peptide exit tunnel at the other. A UFL1 loop inserts into and remodels the peptidyl transferase centre. These features of UREL suggest a crucial function for UFMylation in the release and recycling of stalled or terminated ribosomes from the ER membrane. In the absence of functional UREL, 60S–SEC61 translocon complexes accumulate at the ER membrane, demonstrating that UFMylation is necessary for releasing SEC61 from 60S subunits. Notably, this release is facilitated by a functional switch of UREL from a ‘writer’ to a ‘reader’ module that recognizes its product—UFMylated 60S ribosomes. Collectively, we identify a fundamental role for UREL in dissociating 60S subunits from the SEC61 translocon and the basis for UFMylation in regulating protein homeostasis at the ER.</p

The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons

Stalled ribosomes at the endoplasmic reticulum (ER) are covalently modified with the ubiquitin-like protein UFM1 on the 60S ribosomal subunit protein RPL26 (also known as uL24) 1,2. This modification, which is known as UFMylation, is orchestrated by the UFM1 ribosome E3 ligase (UREL) complex, comprising UFL1, UFBP1 and CDK5RAP3 (ref. 3). However, the catalytic mechanism of UREL and the functional consequences of UFMylation are unclear. Here we present cryo-electron microscopy structures of UREL bound to 60S ribosomes, revealing the basis of its substrate specificity. UREL wraps around the 60S subunit to form a C-shaped clamp architecture that blocks the tRNA-binding sites at one end, and the peptide exit tunnel at the other. A UFL1 loop inserts into and remodels the peptidyl transferase centre. These features of UREL suggest a crucial function for UFMylation in the release and recycling of stalled or terminated ribosomes from the ER membrane. In the absence of functional UREL, 60S–SEC61 translocon complexes accumulate at the ER membrane, demonstrating that UFMylation is necessary for releasing SEC61 from 60S subunits. Notably, this release is facilitated by a functional switch of UREL from a ‘writer’ to a ‘reader’ module that recognizes its product—UFMylated 60S ribosomes. Collectively, we identify a fundamental role for UREL in dissociating 60S subunits from the SEC61 translocon and the basis for UFMylation in regulating protein homeostasis at the ER.</p

The DUF1669 domain of FAM83 family proteins anchor casein kinase 1 isoforms

Members of the casein kinase 1 (CK1) family of serine-threonine protein kinases are implicated in the regulation of many cellular processes, including the cell cycle, circadian rhythms, and Wnt and Hedgehog signaling. Because these kinases exhibit constitutive activity in biochemical assays, it is likely that their activity in cells is controlled by subcellular localization, interactions with inhibitory proteins, targeted degradation, or combinations of these mechanisms. We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A to FAM83H) interacted with the α and α-like isoforms of CK1; FAM83A, FAM83B, FAM83E, and FAM83H also interacted with the δ and ε isoforms of CK1. We detected no interaction between any FAM83 member and the related CK1γ1, CK1γ2, and CK1γ3 isoforms. Each FAM83 protein exhibited a distinct pattern of subcellular distribution and colocalized with the CK1 isoform(s) to which it bound. The interaction of FAM83 proteins with CK1 isoforms was mediated by the conserved domain of unknown function 1669 (DUF1669) that characterizes the FAM83 family. Mutations in FAM83 proteins that prevented them from binding to CK1 interfered with the proper subcellular localization and cellular functions of both the FAM83 proteins and their CK1 binding partners. On the basis of its function, we propose that DUF1669 be renamed the polypeptide anchor of CK1 domain

Growth promoting activities of antagonistic bacterial endophytes from Hevea brasiliensis (Willd. ex A.Juss.) Müll.Arg.

Rubber plantations are known to udergo various biotic and abiotic stresses. However, the symbiotic bacterial endophytes that inhabit them provide protection. Here, we isolated bacterial endophytes from the rubber tree, Hevea brasiliensis (Willd. ex A.Juss.) Müll.Arg. and studied their antagonistic activity against major pathogens such as Phytophthora meadii, Corynespora cassiicola and Corticium salmonicolar. The antifungal metabolites such as HCN, siderophores and salicylic acid were produced by the antagonistic endophytes under in vitro conditions. Bioassay showed the growth promotion by a consortium of selected antagonistic endophytes in H. brasiliensis seedlings. The photosynthetic efficiency of seedlings increased after endophyte inoculation. Endophyte-treated plants showed accumulation of starch granules in root tissues. The selected antagonistic isolates belong to Bacillus sp. and Pseudomonas sp. The study revealed the biocontrol and growth promoting potential of bacterial endophytes from H. brasiliensi

Growth promoting activities of antagonistic bacterial endophytes from Hevea brasiliensis (Willd. ex A.Juss.) Müll.Arg.

827-833Rubber plantations are known to udergo various biotic and abiotic stresses. However, the symbiotic bacterial endophytes that inhabit them provide protection. Here, we isolated bacterial endophytes from the rubber tree, Hevea brasiliensis (Willd. ex A.Juss.) Müll.Arg. and studied their antagonistic activity against major pathogens such as Phytophthora meadii, Corynespora cassiicola and Corticium salmonicolar. The antifungal metabolites such as HCN, siderophores and salicylic acid were produced by the antagonistic endophytes under in vitro conditions. Bioassay showed the growth promotion by a consortium of selected antagonistic endophytes in H. brasiliensis seedlings. The photosynthetic efficiency of seedlings increased after endophyte inoculation. Endophyte-treated plants showed accumulation of starch granules in root tissues. The selected antagonistic isolates belong to Bacillus sp. and Pseudomonas sp. The study revealed the biocontrol and growth promoting potential of bacterial endophytes from H. brasiliensis