SummaryUsing a simple oligo selection procedure, we have previously identified a tobacco sequence-specific DNAbinding activity, TDBA12, that increases markedly during the tobacco mosaic virus (TMV)-induced hypersensitive response (HR). Based on the binding specificity and the two cDNA clones isolated, TDBA12 is related to a novel class of DNA-binding factors containing WRKY domains. In the present study, we report that TDBA12 could be induced not only by TMV infection but also by treatment with salicylic acid (SA) or its biologically active analogs capable of inducing pathogenesis-related (PR) genes and enhanced resistance. TDBA12 was sensitive to temperature and the protein dissociating agent sodium deoxycholate, suggesting that it may be a multimeric factor in which protein-protein interaction is important for the enhanced DNA-binding activity. Pre-treatment of nuclear extracts with alkaline phosphatase abolished TDBA12, suggesting that protein phosphorylation is important for its high DNA-binding activity. TDBA12 specifically recognized the elicitor response element of the tobacco class I basic chitinase gene promoter. The increase in the levels of TDBA12 following TMV infection or SA treatment preceded the induced expression of the tobacco chitinase gene. These results strongly suggest that certain WRKY DNAbinding proteins may be activated by enhanced protein phosphorylation and regulate inducible expression of defense-related genes during pathogen-and SA-induced plant defense responses.
Sensitivity and pressure range are two significant parameters of pressure sensors. Existing pressure sensors have difficulty achieving both high sensitivity and a wide pressure range. Therefore, we propose a new pressure sensor with a ternary nanocomposite Fe2O3/C@SnO2. The sea urchin-like Fe2O3 structure promotes signal transduction and protects Fe2O3 needles from mechanical breaking, while the acetylene carbon black improves the conductivity of Fe2O3. Moreover, one part of the SnO2 nanoparticles adheres to the surfaces of Fe2O3 needles and forms Fe2O3/SnO2 heterostructures, while its other part disperses into the carbon layer to form SnO2@C structure. Collectively, the synergistic effects of the three structures (Fe2O3/C, Fe2O3/SnO2 and SnO2@C) improves on the limited pressure response range of a single structure. The experimental results demonstrate that the Fe2O3/C@SnO2 pressure sensor exhibits high sensitivity (680 kPa−1), fast response (10 ms), broad range (up to 150 kPa), and good reproducibility (over 3500 cycles under a pressure of 110 kPa), implying that the new pressure sensor has wide application prospects especially in wearable electronic devices and health monitoring.
The serine/threonine kinase pim-1 mRNA contains a long and G/C rich 5′-untranslated region (5′-UTR). Previous work suggested that the pim-1 5′-UTR harbors an internal ribosomal entry site (IRES) allowing for internal initiation of translation. However, several previously reported eukaryotic IRES elements actually contain cryptic promoter activity. To test whether an IRES or a cryptic promoter is present in the pim-1 5′-UTR, the 5′-UTR was re-examined using stringent test procedures. Our results show the presence of strong promoter activity in the DNA sequence corresponding to the pim-1 5′-UTR. Both promoterless dicistronic test and northern blot analysis show transcripts being derived from the cryptic promoter in the pim-1 5′-UTR sequence. This cryptic promoter is active in all cell types tested, including Cos-7, NIH3T3, HEK293, Jurkat and K562 cells. When a dicistronic mRNA containing the pim-1 5′-UTR was translated in vitro or in vivo, no IRES activity could be detected. However, the control IRESs from both human rhinovirus and encephalomyocarditis virus exhibited strong IRES activities. In addition, both the RNase protection assay and the 5′-RACE assay detected endogenous pim-1 transcripts with shorter 5′-UTRs. Our data strongly suggest that the IRES activity reported earlier for the pim-1 5′-UTR sequence is due to cryptic promoter activity.
In plants, both abscisic acid (ABA) dependent and independent pathways form the basis for the response to environmental stresses. Sucrose non-fermenting 1-related protein kinase 2 (SnRK2) plays a central role in plant stress signal transduction. However, complete annotation and specific expression patterns of SnRK2s in sugarcane remain unclear. For the present study, we performed a full-length cDNA library survey of sugarcane, thus identifying ten SoSnRK2 genes via phylogenetic, local BLAST methods, and various bioinformatics analyses. Phylogenetic analysis indicated division of SoSnRK2 genes into three subgroups, similar to other plant species. Gene structure comparison with Arabidopsis suggested a unique evolutionary imprint of the SnRK2 gene family in sugarcane. Both sequence alignment and structural annotation provided an overview of the conserved N-terminal and variations of the C-terminal, suggesting functional divergence. Transcript and transient expression assays revealed SoSnRK2s to be involved in the responses to diverse stress signals, and strong ABA induction of SoSnRK2s in subgroup III. Co-expression network analyses indicated the existence of both conserved and variable biological functions among different SoSnRK2s members. In summary, this comprehensive analysis will facilitate further studies of the SoSnRK2 family and provide useful information for the functional validation of SoSnRK2s.
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