PFB0595w is a Plasmodium falciparum J protein that co-localizes with PfHsp70-1 and can stimulate its in vitro ATP hydrolysis activity.

Heat shock proteins, many of which function as molecular chaperones, play important roles in the lifecycle and pathogenesis of the malaria parasite, Plasmodium falciparum. The P. falciparum heat shock protein 70 (PfHsp70) family of chaperones is potentially regulated by a large complement of J proteins that localize to various intracellular compartments including the infected erythrocyte cytosol. While PfHsp70-1 has been shown to be an abundant cytosolic chaperone, its regulation by J proteins is poorly understood. In this study, we characterized the J protein PFB0595w, a homologue of the well-studied yeast cytosolic J protein, Sis1. PFB0595w, similarly to PfHsp70-1, was localized to the parasite cytosol and its expression was upregulated by heat shock. Additionally, recombinant PFB0595w was shown to be dimeric and to stimulate the in vitro ATPase activity of PfHsp70-1. Overall, the expression, localization and biochemical data for PFB0595w suggest that it may function as a cochaperone of PfHsp70-1, and advances current knowledge on the chaperone machinery of the parasite.

Characterization of kinetic coarsening in a random-field Ising model.

We report a study of nonequilibrium relaxation in a two-dimensional random field Ising model at a nonzero temperature. We attempt to observe the coarsening from a different perspective with a particular focus on three dynamical quantities that characterize the kinetic coarsening. We provide a simple generalized scaling relation of coarsening supported by numerical results. The excellent data collapse of the dynamical quantities justifies our proposition. The scaling relation corroborates the recent observation that the average linear domain size satisfies different scaling behavior in different time regimes.

Dynamical properties of random-field Ising model.

Extensive Monte Carlo simulations are performed on a two-dimensional random field Ising model. The purpose of the present work is to study the disorder-induced changes in the properties of disordered spin systems. The time evolution of the domain growth, the order parameter, and the spin-spin correlation functions are studied in the nonequilibrium regime. The dynamical evolution of the order parameter and the domain growth shows a power law scaling with disorder-dependent exponents. It is observed that for weak random fields, the two-dimensional random field Ising model possesses long-range order. Except for weak disorder, exchange interaction never wins over pinning interaction to establish long-range order in the system.

Plasmodium falciparum-encoded exported hsp70/hsp40 chaperone/co-chaperone complexes within the host erythrocyte.

Malaria parasites modify their host cell, the mature human erythrocyte. We are interested in the molecules mediating these processes, and have recently described a family of parasite-encoded heat shock proteins (PfHsp40s) that are targeted to the host cell, and implicated in host cell modification. Hsp40s generally function as co-chaperones of members of the Hsp70 family, and until now it was thought that human Hsp70 acts as the PfHsp40 interaction partner within the host cell. Here we revise this hypothesis, and identify and characterize an exported parasite-encoded Hsp70, referred to as PfHsp70-x. PfHsp70-x is exported to the host erythrocyte where it forms a complex with PfHsp40s in structures known as J-dots, and is closely associated with PfEMP1. Interestingly, Hsp70-x is encoded only by parasite species that export the major virulence factor EMP1, implying a possible role for Hsp70-x in EMP1 presentation at the surface of the infected erythrocyte. Our data strongly support the presence of parasite-encoded chaperone/co-chaperone complexes within the host erythrocyte, which are involved in protein traffic through the host cell. The host-pathogen interaction within the infected erythrocyte is more complex than previously thought, and is driven notonly by parasite co-chaperones, but also by the parasite-encoded chaperone Hsp70-x itself.

Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop).

Malaria is caused by Plasmodium species, whose transmission to vertebrate hosts is facilitated by mosquito vectors. The transition from the cold blooded mosquito vector to the host represents physiological stress to the parasite, and additionally malaria blood stage infection is characterised by intense fever periods. In recent years, it has become clear that heat shock proteins play an essential role during the parasite's life cycle. Plasmodium falciparum expresses two prominent heat shock proteins: heat shock protein 70 (PfHsp70) and heat shock protein 90 (PfHsp90). Both of these proteins have been implicated in the development and pathogenesis of malaria. In eukaryotes, Hsp70 and Hsp90 proteins are functionally linked by an essential adaptor protein known as the Hsp70-Hsp90 organising protein (Hop). In this study, recombinant P. falciparum Hop (PfHop) was heterologously produced in E. coli and purified by nickel affinity chromatography. Using specific anti-PfHop antisera, the expression and localisation of PfHop in P. falciparum was investigated. PfHop was shown to co-localise with PfHsp70 and PfHsp90 in parasites at the trophozoite stage. Gel filtration and co-immunoprecipitation experiments suggested that PfHop was present in a complex together with PfHsp70 and PfHsp90. The association of PfHop with both PfHsp70 and PfHsp90 suggests that this protein may mediate the functional interaction between the two chaperones.

Multifractal behavior of the surfaces evolved with surface relaxation.

A discrete model exhibiting conserved dynamics with nonconserved noise involving particles of different nature, termed as linear and nonlinear, is proposed here. The morphology of the surface has been studied with different abundances of these particles. The saturated surface, slowly evolved from a lower contribution of nonlinear particles to a higher contribution of nonlinear particles, splits into four distinct scaling regimes with three crossover lengths. Each regime is characterized by different scaling property. It is shown that when the contribution of the nonlinear particles crosses a critical value, the surface morphology shows a linear-nonlinear "phase transition." The roughness exponent in a nonlinear regime is well compared with that of the continuum nonlinear equation in a molecular beam epitaxy (MBE) class as well as a MBE motivated discrete model.