39,670 research outputs found

    Temporal and Spectral Correlations of Cyg X-1

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    Temporal and spectral properties of X-ray rapid variability of Cyg X-1 are studied by an approach of correlation analysis in the time domain on different time scales. The correlation coefficients between the total intensity in 2-60 keV and the hardness ratio of 13-60 keV to 2-6 keV band on the time scale of about 1 ms are always negative in all states. For soft states, the correlation coefficients are positive on all the time scales from about 0.01 s to 100 s, which is significantly different with that for transition and low states. Temporal structures in high energy band are narrower than that in low energy band in quite a few cases. The delay of high energy photons relative to low energy ones in the X-ray variations has also been revealed by the correlation analysis. The implication of observed temporal and spectral characteristics to the production region and mechanism of Cyg X-1 X-ray variations is discussed.Comment: 17 pages, 6 figures included, to appear in Ap

    KDM2B/FBXL10 targets c-Fos for ubiquitylation and degradation in response to mitogenic stimulation.

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    KDM2B (also known as FBXL10) controls stem cell self-renewal, somatic cell reprogramming and senescence, and tumorigenesis. KDM2B contains multiple functional domains, including a JmjC domain that catalyzes H3K36 demethylation and a CxxC zinc-finger that recognizes CpG islands and recruits the polycomb repressive complex 1. Here, we report that KDM2B, via its F-box domain, functions as a subunit of the CUL1-RING ubiquitin ligase (CRL1/SCF(KDM2B)) complex. KDM2B targets c-Fos for polyubiquitylation and regulates c-Fos protein levels. Unlike the phosphorylation of other SCF (SKP1-CUL1-F-box)/CRL1 substrates that promotes substrates binding to F-box, epidermal growth factor (EGF)-induced c-Fos S374 phosphorylation dissociates c-Fos from KDM2B and stabilizes c-Fos protein. Non-phosphorylatable and phosphomimetic mutations at S374 result in c-Fos protein which cannot be induced by EGF or accumulates constitutively and lead to decreased or increased cell proliferation, respectively. Multiple tumor-derived KDM2B mutations impaired the function of KDM2B to target c-Fos degradation and to suppress cell proliferation. These results reveal a novel function of KDM2B in the negative regulation of cell proliferation by assembling an E3 ligase to targeting c-Fos protein degradation that is antagonized by mitogenic stimulations

    Escherichia coli of sequence type 3835 carrying blaNDM-1, blaCTX-M-15, blaCMY-42 and blaSHV-12

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    New Delhi metallo-β-lactamase (NDM) represents a serious challenge for treatment and public health. A carbapenem-resistant Escherichia coli clinical strain WCHEC13-8 was subjected to antimicrobial susceptibility tests, whole genome sequencing and conjugation experiments. It was resistant to imipenem (MIC, >256 μg/ml) and meropenem (MIC, 128 μg/ml) and belonged to ST3835. blaNDM-1 was the only carbapenemase gene detected. Strain WCHEC13-8 also had a plasmid-borne AmpC gene (blaCMY-42) and two extended-spectrum β-lactamase genes (blaCTX-M-15 and blaSHV-12). blaNDM-1 and blaSHV-12 were carried by a 54-kb IncX3 self-transmissible plasmid, which is identical to plasmid pNDM-HF727 from Enterobacter cloacae. blaCMY-42 was carried by a 64-kb IncI1 plasmid and blaCTX-M-15 was located on a 141-kb plasmid with multiple F replicons (replicon type: F36:A4:B1). blaCMY-42 was in a complicated context and the mobilisation of blaCMY-42 was due to the transposition of IS Ecp1 by misidentifying its right-end boundary. Genetic context of blaNDM-1 in strain WCHEC13-8 was closely related to those on IncX3 plasmids in various Enterobacteriaceae species in China. In conclusion, a multidrug-resistant ST3835 E. coli clinical strain carrying blaNDM-1, blaCTX-M-15, blaCMY-42 and blaSHV-12 was identified. IncX3 plasmids may be making a significant contribution to the dissemination of blaNDM among Enterobacteriaceae in China
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