Flowering ecology of honey-producing flora in South-East Australia

This report examines the flowering ecology (flowering patterns and the production of floral resources, i.e. nectar and pollen) of important Australian melliferous (honey-producing) flora. Aspects of flowering ecology that can have a negative impact on invertebrates, including honeybees, were also investigated. The research was based on information sourced by highly experienced, commercial beekeepers and, so, provides a valuable written record of long-term observations relating to flowering ecology which otherwise may be lost following the death of beekeepers. Results of this study are of far-reaching importance, not only to the beekeeping industry, but to land managers, the general public and the future of Australian flora and fauna.

An understanding of flowering ecology is vital for many reasons, including implementing appropriate management practices which ensure the sustainability and growth of natural resources and industries like the beekeeping industry. Despite the importance of such studies, very little research has considered flowering ecology in Australian flora. Furthermore, research often was based on short-term data; long-term data are widely acknowledged as being necessary in such research in order to determine ‘real’ flowering patterns. Thus, studies of flowering ecology which use long-term data are vital.

Flowering ecology of south-east Australian melliferous flora

The flowering ecology of south-east Australian melliferous (honey) flora was studied, using observational data from our most experienced beekeepers. Short-term variation and long-term trends were observed which may have critical ecological implications. The study is a significant contribution to flowering ecology and provides an important foundation to guide future research.

Google hacking defence based on honey pages

 Many web servers contain some dangerous pages (we name them eigenpages) that can indicate their vulnerabilities. Therefore, some worms such as Santy locate their targets by searching for these eigenpages in search engines with well-crafted queries. In this paper, we focus on the modeling and containment of these special worms targeting web applications. We propose a containment system based on honey pots. We make search engines randomly insert a few honey pages that will induce visitors to the pre-established honey pots among the search results for the arriving queries. And then infectious can be detected and reported to the search engines when their malicious scans hit the honey pots. We find that the Santy worm can be well stopped by inserting no more than two honey pages in every one hundred search results. We also solve the challenging issue to dynamically generate matching honey pages for those dynamically arriving queries. Finally, a prototype is implemented to prove the technical feasibility of this system. © 2013 by CESER Publications.

An improved Gbest guided artificial bee colony (IGGABC) algorithm for classification and prediction tasks

Artificial Neural Networks (ANN) performance depends on network topology, activation function, behaviors of data, suitable synapse's values and learning algorithms. Many existing works used different learning algorithms to train ANN for getting high performance. Artificial Bee Colony (ABC) algorithm is one of the latest successfully Swarm Intelligence based technique for training Multilayer Perceptron (MLP). Normally Gbest Guided Artificial Bee Colony (GGABC) algorithm has strong exploitation process for solving mathematical problems, however the poor exploration creates problems like slow convergence and trapping in local minima. In this paper, the Improved Gbest Guided Artificial Bee Colony (IGGABC) algorithm is proposed for finding global optima. The proposed IGGABC algorithm has strong exploitation and exploration processes. The experimental results show that IGGABC algorithm performs better than that standard GGABC, BP and ABC algorithms for Boolean data classification and time-series prediction tasks.

Long-term flowering patterns of melliferous Eucalyptus (Myrtaceae) species

The flowering patterns of 28 Victorian melliferous (honey-producing) eucalypts were investigated by using long-term observations of highly experienced, commercial apiarists. Frequency, timing, duration and intensity of flowering were determined, as were spatial differences within and among species. Data were obtained by face-to-face interviews with 25 Victorian apiarists, each of whom had operated a minimum of 350 hives for a minimum of 30 years. Flowering frequency ranged from 1 to 7 years, and most species flowered once every 2–4 years. Long-term flowering frequency, timing and duration were reported as constant, although short-term perturbations could occur. Most melliferous species flowered during spring and summer for a period of 3 months or more. Only few species had shorter flowering periods. Information provided by apiarists compared well with available published information (e.g. flowering period reported in field guides) and revealed a reliable, largely untapped source of long-term data, the use of which could benefit many ecological research endeavours.

2D and 3D modelling of building form subjected to ember attack

This paper furthers the research of Rollo, Luther and Atkinson 1999, and Rollo, Honey, Atkinson and Luther 2003, regarding the way in which building shape appears to contribute to the collection of fire-brand debris subject to ember attack. The paper will present a range of 2D fluid-mapping and 3D wind tunnel studies (Melaragno 1982) which have been correlated with the transportation characteristics of an ember laden air-field (Cheney and Sullivan 1997). Working with a range of generic building types the paper also introduces simple spatial modelling techniques which are being developed to illustrate the relationship between ember capture and changes in wind speed and air pressure.

The last 10 amino acid residues beyond the hydrophobic motif are critical for the catalytic competence and function of protein kinase Cá*

The segment C-terminal to the hydrophobic motif at the V5 domain of protein kinase C (PKC) is the least conserved both in length and in amino acid identity among all PKC isozymes. By generating serial truncation mutants followed by biochemical and functional analyses, we show here that the very C terminus of PKCα is critical in conferring the full catalytic competence to the kinase and for transducing signals in cells. Deletion of one C-terminal amino acid residue caused the loss of ~60% of the catalytic activity of the mutant PKCα, whereas deletion of 10 C-terminal amino acid residues abrogated the catalytic activity of PKCα in immune complex kinase assays. The PKCα C-terminal truncation mutants were found to lose their ability to activate mitogen-activated protein kinase, to rescue apoptosis induced by the inhibition of endogenous PKC in COS cells, and to augment melatonin-stimulated neurite outgrowth. Furthermore, molecular dynamics simulations revealed that the deletion of 1 or 10 C-terminal residues results in the deformation of the V5 domain and the ATP-binding pocket, respectively. Finally, PKCα immunoprecipitated using an antibody against its C terminus had only marginal catalytic activity compared with that of the PKCα immunoprecipitated by an antibody against its N terminus. Therefore, the very C-terminal tail of PKCα is a novel determinant of the catalytic activity of PKC and a promising target for selective modulation of PKCα function. Molecules that bind preferentially to the very C terminus of distinct PKC isozymes and suppress their catalytic activity may constitute a new class of selective inhibitors of PKC.

Identification of an integral plasma membrane pool of protein kinase C in mammalian tissues and cells

Protein kinase C (PKC) is a family of serine/threonine protein kinases that are pivotal in cellular regulation. Since its discovery in 1977, PKCs have been known as cytosolic and peripheral membrane proteins. However, there are reports that PKC can insert into phospholipids vesicles in vitro. Given the intimate relationship between the plasma membrane and the activation of PKC, it is important to determine whether such “membrane-inserted” form of PKC exists in mammalian cells or tissues. Here, we report the identification of an integral plasma membrane pool for all the 10 PKC isozymes in vivo by their ability to partition into the detergent-rich phase in Triton X-114 phase partitioning, and by their resistance to extractions with 0.2 M sodium carbonate (pH 11.5), 2 M urea and 2 M sodium chloride. The endogenous integral membrane pool of PKC in mouse fibroblasts is found to be acutely regulated by phorbol ester or diacylglycerol, suggesting that this pool of PKC may participate in cellular processes known to be regulated by PKC. At least for PKCα, the C2–V3 region at the regulatory domain of the kinase is responsible for membrane integration. Further exploration of the function of this novel integral plasma membrane pool of PKC will not only shed new light on molecular mechanisms underlying its cellular functions but also provide new strategies for pharmaceutical modulation of this important group of kinases.

The PKCÁ-D294G mutant found in pituitary and thyroid tumors fails to transduce extracellular signals

Protein kinase C (PKC) is a key regulator of cell proliferation, differentiation, and apoptosis and is one of the drug targets of anticancer therapy. Recently, a single point mutation (D294G) in PKCα has been found in pituitary and thyroid tumors with more invasive phenotype. Although the PKCα-D294G mutant is implicated in the progression of endocrine tumors, no apparent biochemical/cell biological abnormalities underlying tumorigenesis with this mutant have been found. We report here that the PKCα-D294G mutant is unable to bind to cellular membranes tightly despite the fact that it translocates to the membrane as efficiently as the wild-type PKCα upon treatment of phorbol ester. The impaired membrane binding is associated with this mutant's inability to transduce several antitumorigenic signals as it fails to mediate phorbol ester–stimulated translocation of myristoylated alanine–rich protein kinase C substrate (MARCKS), to activate mitogen-activated protein kinase and to augment melatonin-stimulated neurite outgrowth. Thus, the PKCα-D294G is a loss-of-function mutation. We propose that the wild-type PKCα may play important antitumorigenic roles in the progression of endocrine tumors. Therefore, developing selective activators instead of inhibitors of PKCα might provide effective pharmacological interventions for the treatment of certain endocrine tumors.

The very C-terminus of protein kinase CĹ is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1

In this article, we explore the role of the C-terminus (V5 domain) of PKCvar epsilon plays in the catalytic competence of the kinase using serial truncations followed by immune-complex kinase assays. Surprisingly, removal of the last seven amino acid residues at the C-terminus of PKCvar epsilon resulted in a PKCvar epsilon-Δ731 mutant with greatly reduced intrinsic catalytic activity while truncation of eight amino acid residues at the C-terminus resulted in a catalytically inactive PKCvar epsilon mutant. Computer modeling and molecular dynamics simulations showed that the last seven and/or eight amino acid residues of PKCvar epsilon were involved in interactions with residues in the catalytic core. Further truncation analyses revealed that the hydrophobic phosphorylation motif was dispensable for the physical interaction between PKCvar epsilon and 3-phosphoinositide-dependent kinase-1 (PDK-1) as the PKCvar epsilon mutant lacking both the turn and the hydrophobic motifs could still be co-immunoprecipitated with PDK-1. These results provide fresh insights into the biochemical and structural basis underlying the isozyme-specific regulation of PKC and suggest that the very C-termini of PKCs constitute a promising new target for the development of novel isozyme-specific inhibitors of PKC.

The last five amino acid residues at the C-terminus of PRK1 /KKN is essential for full lipid responsiveness

PRK1/PKN is a member of the protein kinase C (PKC) superfamily of serine/threonine protein kinases. Despite its important role as a RhoA effector, limited information is available regarding how this kinase is regulated. We show here that the last seven amino acid residues at the C-terminus is dispensable for the catalytic activity of PRK1 but is critical for the in vivo stability of this kinase. Surprisingly, the intact hydrophobic motif in PRK1 is dispensable for 3-phosphoinositide-dependent kinase-1 (PDK-1) binding and phosphorylation of the activation loop, as the PRK1-Δ940 mutant lacking the last two residues of the hydrophobic motif and the last 5 residues at the C-terminus interacts with PDK-1 in vivo and has a similar specific activity as the wild-type protein. We also found that the last four amino acid residues at the C-terminus of PRK1 is critical for the full lipid responsiveness as the PRK1-Δ942 deletion mutant is no longer activated by arachidonic acid. Our data suggest that the very C-terminus in PRK1 is critically involved in the control of the catalytic activity and activation by lipids. Since this very C-terminal segment is the least conserved among members of the PKC superfamily, it would be a promising target for isozyme-specific pharmaceutical interventions.

The very C-terminus of PRK1/PKN is essential for its activation by RhoA and downstream signaling

PRK1 is a lipid- and Rho GTPase-activated serine/threonine protein kinase implicated in the regulation of receptor trafficking, cytoskeletal dynamics and tumorigenesis. Although Rho binding has been mapped to the HR1 region in the regulatory domain of PRK1, the mechanism involved in the control of PRK1 activation following Rho binding is poorly understood. We now provide the first evidence that the very C-terminus beyond the hydrophobic motif in PRK1 is essential for the activation of this kinase by RhoA. Deletion of the HR1 region did not completely abolish the binding of PRK1-ΔHR1 to GTPγS-RhoA nor the activation of this mutant by GTPγS-RhoA in vitro. In contrast, removing of the last six amino acid residues from the C-terminus of PRK1 or truncating of a single C-terminal residue from PRK1-ΔHR1 completely abrogated the activation of these mutants by RhoA both in vitro and in vivo. The critical dependence of the very C-terminus of PRK1 on the signaling downstream of RhoA was further demonstrated by the failure of the PRK1 mutant lacking its six C-terminal residues to augment lisophosphatidic acid-elicited neurite retraction in neuronal cells. Thus, we show that the HR1 region is necessary but not sufficient in eliciting a full activation of PRK1 upon binding of RhoA. Instead, such activation is controlled by the very C-terminus of PRK1. Our results also suggest that the very C-terminus of PRK1, which is the least conserved among members of the protein kinase C superfamily, is a potential drug target for pharmacological intervention of RhoA-mediated signaling pathways