GmIAA27 Encodes an AUX/IAA Protein Involved in Dwarfing and Multi-Branching in Soybean

Soybean plant height and branching affect plant architecture and yield potential in soybean. In this study, the mutant dmbn was obtained by treating the cultivar Zhongpin 661 with ethylmethane sulfonate. The dmbn mutant plants were shorter and more branched than the wild type. The genetic analysis showed that the mutant trait was controlled by a semi-dominant gene. The candidate gene was fine-mapped to a 91 kb interval on Chromosome 9 by combining BSA-seq and linkage analysis. Sequence analysis revealed that Glyma.09g193000 encoding an Aux/IAA protein (GmIAA27) was mutated from C to T in the second exon of the coding region, resulting to amino acid substitution of proline to leucine. Overexpression of the mutant type of this gene in Arabidopsis thaliana inhibited apical dominance and promoted lateral branch development. Expression analysis of GmIAA27 and auxin response genes revealed that some GH3 genes were induced. GmIAA27 relies on auxin to interact with TIR1, whereas Gmiaa27 cannot interact with TIR1 owing to the mutation in the degron motif. Identification of this unique gene that controls soybean plant height and branch development provides a basis for investigating the mechanisms regulating soybean plant architecture development.     

Reduced VDAC1, Maintained Mitochondrial Dynamics and Enhanced Mitochondrial Biogenesis in a Transgenic Tau Mouse Model of Alzheimer’s Disease

Alzheimer’s disease (AD) is one of the most common forms of neurodegeneration, defined by reduced cognitive function, which is caused by the gradual death of neurons in the brain. Recent studies have shown an age-dependent rise in the levels of voltage-dependent anion channel 1 (VDAC1) in AD. In addition, we discovered an aberrant interaction between VDAC1 and P-TAU in the brains of AD patients, which led to abnormalities in the structural and functional integrity of the mitochondria. The purpose of our study is to understand the protective effects of reduced VDAC1 against impaired mitochondrial dynamics and defective mitochondrial biogenesis in transgenic TAU mice. Recently, we crossed heterozygote VDAC1 knockout (VDAC1^+/−) mice with transgenic TAU mice to obtain double-mutant VDAC1^+/−/TAU mice. Our goal was to evaluate whether a partial decrease in VDAC1 lessens the amount of mitochondrial toxicity in transgenic Tau (P301L) mice. We found that mitochondrial fission proteins were significantly reduced, and mitochondrial fusion and biogenesis proteins were increased in double-mutant mice compared to TAU mice. On the basis of these discoveries, the current work may have significance for the development of reduced-VDAC1-based treatments for individuals suffering from AD as well as other tauopathies.     

一种改进型的OPA密写算法

最佳奇偶分配密写（OPA）是针对调色板图像密写中的一种低失真、高隐蔽性的方法。首先对OPA算法及其分析算法进行了深入研究。并针对颜色混乱分析提出了一种新型OPA算法,该算法引入亮度分量参与颜色的奇偶分配,能够有效兼顾密写信息容量和信息安全的双方面要求。最后,还提出利用SHA-1算法完成新密写算法的伪随机游走写入,进一步提高了密写过程的安全性和隐蔽性。     

内蒙古大兴安岭根河植被覆盖度动态变化及影响因素的分析

研究植被覆盖度（Fractional Vegetation Cover,FVC）动态变化,可增强了解森林群落的抵抗力和恢复力,为森林生态系统定量评价提供科学依据。基于像元二分模型、Landsat-5 TM（2006、2010）及高分一号（GF-1,2016）数据估算了3个时期的根河市FVC,引入变化率和动态度2个指标评价其动态变化情况,并且分析了多因素对该变化的影响。实验结果显示：中度以上等级占总面积80%以上,2016年低、较低、中度、较高、高等级FVC分别为1 645.02、1 655.97、3 536.59、5 556.87、7507.15 km²。采用0.2 m航空CCD影像进行植被/非植被点提取后,针对2016年的FVC估算结果进行交叉验证的精度为0.92。变化分析结果显示：除部分地区外（敖鲁古雅）,2006~2016 年间FVC变化整体上呈增加态,尤其是高等级增加了1 668.78 km²。综合来看,根河市植被覆盖良好,多重因素共同影响其动态变化,局部FVC对火灾干扰的变化极为敏感,低海拔和平坡FVC明显降低,与人类生产生活密切相关。     

基于改进一维卷积和双向长短期记忆神经网络的故障诊断方法

针对工业领域中故障诊断数据存在时序性和夹杂强噪声的特点导致的收敛速度慢以及诊断精度低的问题,提出了一种基于改进一维卷积和双向长短期记忆（1DCNN-BiLSTM）神经网络融合的故障诊断方法。该方法包括故障振动信号的预处理、特征的自动提取以及振动信号的分类。首先,采用自适应白噪声的完整经验模态分解（CEEMDAN）技术对原始振动信号进行预处理;其次,构建1DCNN-BiLSTM双通道模型,将处理后信号输入双向长短期记忆（BiLSTM）神经网络模型和一维卷积神经网络（1DCNN）模型两个通道,从而对信号的时序相关性特征、局部空间的非相关性特征和弱周期性规律进行充分提取;然后,针对信号夹杂强噪声的问题,对压缩与激励网络（SENet）模块进行改进并将其作用于两个不同的通道;最后,输入全连接层将双通道提取的特征进行融合并借助Softmax分类器实现对设备故障的精确识别。使用凯斯西储大学轴承数据集进行实验,结果表明改进后的SENet模块同时作用于1DCNN通道和stacked BiLSTM通道,1DCNN-BiLSTM双通道模型在保证快速收敛的情况下有最高诊断精度96.87%,优于传统单通道模型,有效提高了机械设备故障诊断效率。     

Neuronal ApoE Regulates the Cell-to-Cell Transmission of α-Synuclein

The presence of protein inclusions, called Lewy bodies (LBs) and Lewy neurites (LNs), in the brain is the main feature of Parkinson’s disease (PD). Recent evidence that the prion-like propagation of α-synuclein (α-syn), as a major component of LBs and LNs, plays an important role in the progression of PD has gained much attention, although the molecular mechanism remains unclear. In this study, we evaluated whether neuronal ApoE regulates the cell-to-cell transmission of α-syn and explored its molecular mechanism using in vitro and in vivo model systems. We demonstrate that neuronal ApoE deficiency attenuates both α-syn uptake and release by downregulating LRP-1 and LDLR expression and enhancing chaperone-mediated autophagy activity, respectively, thereby contributing to α-syn propagation. In addition, we observed that α-syn propagation was attenuated in ApoE knockout mice injected with pre-formed mouse α-syn fibrils. This study will help our understanding of the molecular mechanisms underlying α-syn propagation.     

Reg-1α, a New Substrate of Calpain-2 Depending on Its Glycosylation Status

Reg-1α/lithostathine, a protein mainly associated with the digestive system, was previously shown to be overexpressed in the pre-clinical stages of Alzheimer’s disease. In vitro, the glycosylated protein was reported to form fibrils at physiological pH following the proteolytic action of trypsin. However, the nature of the protease able to act in the central nervous system is unknown. In the present study, we showed that Reg-1α can be cleaved in vitro by calpain-2, the calcium activated neutral protease, overexpressed in neurodegenerative diseases. Using chemical crosslinking experiments, we found that the two proteins can interact with each other. Identification of the cleavage site using mass spectrometry, between Gln⁴ and Thr⁵, was found in agreement with the in silico prediction of the calpain cleavage site, in a position different from the one reported for trypsin, i.e., Arg¹¹-Ile¹² peptide bond. We showed that the cleavage was impeded by the presence of the neighboring glycosylation of Thr⁵. Moreover, in vitro studies using electron microscopy showed that calpain-cleaved protein does not form fibrils as observed after trypsin cleavage. Collectively, our results show that calpain-2 cleaves Reg-1α in vitro, and that this action is not associated with fibril formation.