The MDM2 RING Domain and Central Acidic Domain Play Distinct Roles in MDM2 Protein Homodimerization and MDM2-MDMX Protein Heterodimerization

The oncoprotein murine double minute 2 (MDM2) is an E3 ligase that plays a prominent role in p53 suppression by promoting its polyubiquitination and proteasomal degradation. In its active form, MDM2 forms homodimers as well as heterodimers with the homologous protein murine double minute 4 (MDMX), both of which are thought to occur through their respective C-terminal RING (really interesting new gene) domains. In this study, using multiple MDM2 mutants, we show evidence suggesting that MDM2 homo- and heterodimerization occur through distinct mechanisms because MDM2 RING domain mutations that inhibit MDM2 interaction with MDMX do not affect MDM2 interaction with WT MDM2. Intriguingly, deletion of a portion of the MDM2 central acidic domain selectively inhibits interaction with MDM2 while leaving intact the ability of MDM2 to interact with MDMX and to ubiquitinate p53. Further analysis of an MDM2 C-terminal deletion mutant reveals that the C-terminal residues of MDM2 are required for both MDM2 and MDMX interaction. Collectively, our results suggest a model in which MDM2-MDMX heterodimerization requires the extreme C terminus and proper RING domain structure of MDM2, whereas MDM2 homodimerization requires the extreme C terminus and the central acidic domain of MDM2, suggesting that MDM2 homo- and heterodimers utilize distinct MDM2 domains. Our study is the first to report mutations capable of separating MDM2 homo- and heterodimerization.     

A protein in rat prostatic interacting with androgen regulated gene

2M NaCl-insoluble fraction of rat ventral prostatechromatin(residual proteins)contain proteins able tointeract specifically with androgen-receptor complex andis,therefore,a part of the acceptor complex.Amongresidual proteins,a 97 KDa protein has been found whichbinds signifieantly to a genomic fragment containingan androgen-regulated gene coding for a 22 KDa protein.The biological significance of this binding in androgenaction need to be further studied. A mini-plasmid clone containing 22 KDa proteincoding sequence was cloned into Charon 4A genomiclibrary from which a 5.7 Kb genomic fragment wasisolated,identified by hybridization with a 5' and a 3'cDNA probes,and shown to contain the 5' flankingsequence.Restriction enzyme treatment of this fragmentyielded a 4.7 Kb restriction fragment representingthe 5' upstream region and a 1.0 Kb containing part ofthe coding sequence.Deletion studies indicated that the97 KDa protein bound only to a subclone of about 300 bpsegment.Furthermore,gel shifting experiment supportedits DNA-prptein binding.     

激光光漂恢复技术测定林蛙卵第一次卵裂前卵表面的运动

激光光漂恢复技术测定了异硫氰基荧光素标记的林蛀卵表面分子在第一次卵裂前的运动。发现固着在玻片上的剥离“细胞膜”的分子运动形式为扩散。扩散系数为(4.6±1.3)×10~(-12)cm~2/s,可动部份为15%。完整卵子上的分子运动形式为流动。细胞膜在不停地流动着。它可能起着协助细胞质运动的作用。细胞膜流动的速度随时间而异,卵裂前不久,在大多数的卵子上,出现两个流动较慢的谷,少数细胞只测到一个谷。这可能与光漂起始时间,光斑与未来分裂沟的距离,和卵子间的差异有关。也讨论了这种速度变化与表面收缩波的关系。     

鼠疫疫苗研究的现状与展望

鼠疫（Plague）是由鼠疫耶尔森菌(Yersina pestis，Y. pestis)（简称鼠疫菌）引起的一种烈性传染病，属甲类传染病，具有高度传染性和致病性。在过去的鼠疫大流行中近2亿感染者死亡。疫苗接种是疾病预防控制的重要方法。现就鼠疫疫苗的研究进展作一综述，为新疫苗的研制提供参考。     

1991-2017年叶尔羌河流域冰川景观格局时空演变

冰川景观变化是全球环境和气候变化的共同"指示器"。随着全球气候变化加剧，干旱和半干旱地区的冰川景观将进一步变化。科学评估冰川景观格局时空演变特征，为应对冰川景观变化及其影响提供科学参考。基于1991-2017年Landsat TM/ETM+/OLI遥感影像，采用监督分类方法获取叶尔羌河流域冰川景观时空格局及变化数据，利用景观格局指数、质心迁移模型、分形维数等方法分析近26年叶尔羌河流域冰川景观格局时空演变特征。结果表明：（1）1991-2017年叶尔羌河流域冰川斑块面积呈消减趋势，但有所减缓，共减少799.50 km²（-13.09%）。冰川斑块面积消减主要集中在海拔5400-5800 m之间，相较之下，海拔4400 m以下的区域冰川斑块面积消减率最高，达63.68%；不同坡度冰川景观消减率存在差异，陡坡冰川斑块面积消减率最高（15.98%），急陡坡消减率最低（2.87%）；阴阳两坡冰川景观均呈消减趋势，阳坡冰川斑块面积消减速率显著高于阴坡。（2）近26年来，叶尔羌河流域冰川斑块数量、最大斑块指数均减小，而平均形状指数、平均周长面积比、分裂指数均增加，表明冰川景观不断消减，破碎化程度增加。（3）研究期间，叶尔羌河流域冰川景观质心发生迁移，整体呈现东北偏移趋势。（4）通过分形理论对叶尔羌河流域冰川景观空间结构特征进行分析表明，该流域冰川景观消减率略微降低，但仍然处于持续消融状态。