RESUMEN
The hybrid of organic conducting polymers and inorganic materials with ultralow thermal conductivity, which is a promising strategy for the realization of polymer based effective thermoelectric (TE) applications. In this work, ultrathin layered molybdenum disulphide (MoS2) nanosheets/PANI nanocomposites are prepared by hydrothermal route. The effect of varying PANI wt% in the nanocomposites and its interface effect on thermoelectric properties are well investigated. The successful incorporation of PANI between the MoS2 layers confirmed by high resolution transmission electron microscope (HRTEM). The significantly enhanced potential difference of MoS2/ PANI nanocomposites with increasing PANI content is well clarified by the increased Seebeck value. The variable range hopping property is identified and conductivity is raised up highly due to insertion of PANI in layered van der Waal's gap of MoS2. The effective interface facilitates charge for fast transport. The reduced thermal conductivity is observed of about 0.248 W*m-1*K-1 for 2.5 wt% addition of PANI. The key factor is that the stability of the sample is improved for MoS2/ PANI nanocomposites than pristine MoS2. Our work paved a new approach to improve TE performance by preparing TE MoS2 material through simple chemical route.
RESUMEN
The mitochondrial phosphate carrier gene (PiC) encodes a membrane protein that mediates the supply of inorganic phosphate from the cytosol into the mitochondrial matrix. This substrate-specific transport system plays an important role in efficient ATP synthesis. Mammals appear to have only one PiC with two alternative splicing variants whose functional differences remain unclear. The present study is the first to characterize the multiple genes that encode PiC in insects. Bombyx mori was found to have two PiC paralogues, one ubiquitous and one testis-specific, the latter seeming to be present only in Lepidoptera. Drosophila melanogaster was found to harbour two PiC paralogues, whereas Liriomyza chinensis, another dipteran, has three PiC paralogues. Two PiCs were found to be present in Plautia stali, and silencing either of these genes affected the normal development of P. stali nymphs, although their expression patterns differed amongst tissues. Schistocerca gregaria and Locusta migratoria have two PiC each, with different expression patterns. Tribolium castaneum was found to have only one PiC, which appears to play an essential role in larval development. Thus, although the inorganic phosphate transport system appears to be conserved across eukaryotes, PiC has become specialized in the different tissues of different insect species.
Asunto(s)
Proteínas de Insectos/metabolismo , Insectos/metabolismo , Proteínas Mitocondriales/metabolismo , Proteínas de Transporte de Fosfato/metabolismo , Animales , Femenino , Proteínas de Insectos/genética , Insectos/genética , Masculino , Proteínas Mitocondriales/genética , Músculos/metabolismo , Proteínas de Transporte de Fosfato/genética , FilogeniaRESUMEN
The Fanconi anaemia (FA) pathway is responsible for interstrand crosslink (ICL) repair. Among the FA core complex components, FANCM is believed to act as a damage sensor for the ICL-blocked replication fork and also as a molecular platform for FA core complex assembly and interaction with Bloom's syndrome (BS) complex that is thought to play an important role in the processing of DNA structures such as stalled replication forks. In the present study, we found that in silkworms, Bombyx mori, a species lacking the major FA core complex components (FANCA, B, C, E, F, and G), FancM is required for FancD2 monoubiquitination and cell proliferation in the presence of mitomycin C (MMC). Silkworm FancM (BmFancM) was phosphorylated in the middle regions, and the modification was associated with its subcellular localization. In addition, BmFancM interacted with Mhf1, a histone-fold protein, and Rmi1, a subunit of the BS complex, in the different regions. The interaction region containing at least these two protein-binding domains played an essential role in FancM-dependent resistance to MMC. Our results suggest that BmFancM also acts as a platform for recruitment of both the FA protein and the BS protein, although the silkworm genome seems to lose FAAP24, a FancM-binding partner protein in mammals.