分类： 物理学 >> 普通物理:统计和量子力学,量子信息等 提交时间： 2018-04-24 合作期刊: 《干旱区科学》
LI, Congjuan
LIU, Ran
WANG, Shijie
SUN, Yongqiang
LI, Shengyu
ZHANG, Heng
GAO, Jie
DANG, Yanxi
ZHANG, Lili
摘要： Extremely saline soils are very harsh environments for the growth and survival of most plant species, however, halophytes can grow well. The underlying mechanism of halophyte to resist high saline is not well understood by us. This study was conducted at the potash mine near the Lop Nur, China, where the effects of the halophyte Suaeda salsa L. on the saline-alkaline soils and its growth and sustainability were investigated. Four plots (in which the salt encrustation layers were removed), with different soil treatments were evaluated: (1) undisturbed soil, with no additional treatment (T1); (2) the slag soil zone, in which a 40-cm layer of slag was placed on the undisturbed soil surface (T2); (3) slag+sandy soil, in which a 20-cm layer of slag was placed in the lower layer and 20 cm of sandy soil, taken from an area about 70 km away from Lop Nur potash mine, where Tamarix species were growing, was placed in the upper layer (T3); and (4) a 40-cm sandy soil layer taken from the area where Tamarix species were growing was placed on undisturbed soil (T4). Soil nutrient contents increased in the four treatments, but salt content only decreased in the T1 treatment. Salt content in the T4 treatment increased over the two-year period, which may be partly attributed to salt deposition from wind-blown dust within the mine and salt accumulation within the surface soil (0–20 cm) in response to high evaporative demands. The S. salsa plants exhibited greater improvements in growth under the T4 treatment than under the T1, T2, and T3 treatments, which demonstrated that low levels of salinity are beneficial for the growth of this species. The T1 treatment was sustainable because of its low cost and superior soil improvement characteristics. Therefore, S. salsa plants not only reduced soil salinity and increased soil nutrient levels, but also ameliorated the plant growth environment, which would be beneficial for both the ecological restoration of the Lop Nur area and similar areas throughout the world.
分类： 生物学 >> 生物物理学 提交时间： 2016-05-11
Gao, Shijuan
Li, Jiandong
Song, Liping
Sheng, Chunjie
Liu, Dong
Jiang, Wei
Chen, Shuai
Huang, Wenlin
Wu, Jiaoxiang
Yao, Chen
Chen, Huiming
Liu, Ran-Yi
Chen, Shuai
Huang, Wenlin
Huang, Wenlin
Teng, Yan
摘要： Influenza A viruses (IAVs) rely on host factors to support their life cycle, as viral proteins hijack or interact with cellular proteins to execute their functions. Identification and understanding of these factors would increase our knowledge of the molecular mechanisms manipulated by the viruses. In this study, we searched for novel binding partners of the influenza A virus NS2 protein, the nuclear export protein responsible for overcoming host range restriction, by a yeast two-hybrid screening assay and glutathione S-transferase-pulldown and coimmunoprecipitation assays and identified AIMP2, a potent tumor suppressor that usually functions to regulate protein stability, as one of the major NS2-binding candidates. We found that the presence of NS2 protected AIMP2 from ubiquitin-mediated degradation in NS2-transfected cells and AIMP2 functioned as a positive regulator of IAV replication. Interestingly, AIMP2 had no significant effect on NS2 but enhanced the stability of the matrix protein M1. Further, we provide evidence that AIMP2 recruitment switches the modification of M1 from ubiquitination to SUMOylation, which occurs on the same attachment site (K242) on M1 and thereby promotes M1-mediated viral ribonucleoprotein complex nuclear export to increase viral replication. Collectively, our results reveal a new mechanism of AIMP2 mediation of influenza virus replication. IMPORTANCE Although the ubiquitination of M1 during IAV infection has been observed, the precise modification site and the molecular consequences of this modification remain obscure. Here, we demonstrate for the first time that ubiquitin and SUMO compete for the same lysine (K242) on M1 and the interaction of NS2 with AIMP2 facilitates the switch of the M1 modification from ubiquitination to SUMOylation, thus increasing viral replication.
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