在Web of Science数据库中,以锻炼心理学作主题词进行检索,并对所得文献数据进行科学图谱分析,梳理国外锻炼心理学研究脉络,以呈现学科研究的热点与前沿。分析表明,国外锻炼心理学在研究者群体中尚未形成研究热点;引领学科研究的团队和...在Web of Science数据库中,以锻炼心理学作主题词进行检索,并对所得文献数据进行科学图谱分析,梳理国外锻炼心理学研究脉络,以呈现学科研究的热点与前沿。分析表明,国外锻炼心理学在研究者群体中尚未形成研究热点;引领学科研究的团队和机构集中在英美两国的著名大学;作为一门应用性学科,锻炼心理学的重要理论基础来源于社会认知心理学,而学科研究的信效度问题成为国外研究者们的焦点议题;锻炼心理学中质性研究和青少年问题成为当前的国外研究前沿。展开更多
CREPT and p15RS are two recently identified homologous proteins that regulate cell proliferation in an opposite way and are closely related to human cancer development.Both CREPT and p15RS consist of an N-terminal RPR...CREPT and p15RS are two recently identified homologous proteins that regulate cell proliferation in an opposite way and are closely related to human cancer development.Both CREPT and p15RS consist of an N-terminal RPR domain and a C-terminal domain with high sequence homology.The transcription enhancement by CREPT is attributed to its interaction with RNA polymerase II(Pol II).Here we provide biochemical and structural evidence to support and extend this molecular mechanism.Through fluorescence polarization analysis,we show that the RPR domains of CREPT and p15RS(CREPT-RPR and p15RS-RPR)bind to different Pol II C-terminal domain(CTD)phosphoisoforms with similar affinity and specificity.We also determined the crystal structure of p15RS-RPR.Sequence and structural comparisons with RPR domain of Rtt103,a homolog of CREPT and p15RS in yeast,reveal structural basis for the similar binding profile of CREPT-RPR and p15RS-RPR with Pol II CTD.We also determined the crystal structure of the C-terminal domain of CREPT(CREPT-CTD),which is a long rod-like dimer and each monomer adopts a coiled-coil structure.We propose that dimerization through the C-terminal domain enhances the binding strength between CREPT or p15RS with Pol II by increasing binding avidity.Our results collectively reveal the respective roles of N-terminal RPR domain and C-terminal domain of CREPT and p15RS in recognizing RNA Pol II.展开更多
文摘在Web of Science数据库中,以锻炼心理学作主题词进行检索,并对所得文献数据进行科学图谱分析,梳理国外锻炼心理学研究脉络,以呈现学科研究的热点与前沿。分析表明,国外锻炼心理学在研究者群体中尚未形成研究热点;引领学科研究的团队和机构集中在英美两国的著名大学;作为一门应用性学科,锻炼心理学的重要理论基础来源于社会认知心理学,而学科研究的信效度问题成为国外研究者们的焦点议题;锻炼心理学中质性研究和青少年问题成为当前的国外研究前沿。
基金supported by Ministry of Science and Technology(2010CB912402 and 2011CB910502)Ministry of Health(2012ZX1000-1009) and the Fok Ying Tung Education Foundation to Wang XinQuan+1 种基金the National Natural Science Foundation of China(81230044,81372167 and 31071225)the Tsinghua Science Foundation(20121080018)to Chang ZhiJie
文摘CREPT and p15RS are two recently identified homologous proteins that regulate cell proliferation in an opposite way and are closely related to human cancer development.Both CREPT and p15RS consist of an N-terminal RPR domain and a C-terminal domain with high sequence homology.The transcription enhancement by CREPT is attributed to its interaction with RNA polymerase II(Pol II).Here we provide biochemical and structural evidence to support and extend this molecular mechanism.Through fluorescence polarization analysis,we show that the RPR domains of CREPT and p15RS(CREPT-RPR and p15RS-RPR)bind to different Pol II C-terminal domain(CTD)phosphoisoforms with similar affinity and specificity.We also determined the crystal structure of p15RS-RPR.Sequence and structural comparisons with RPR domain of Rtt103,a homolog of CREPT and p15RS in yeast,reveal structural basis for the similar binding profile of CREPT-RPR and p15RS-RPR with Pol II CTD.We also determined the crystal structure of the C-terminal domain of CREPT(CREPT-CTD),which is a long rod-like dimer and each monomer adopts a coiled-coil structure.We propose that dimerization through the C-terminal domain enhances the binding strength between CREPT or p15RS with Pol II by increasing binding avidity.Our results collectively reveal the respective roles of N-terminal RPR domain and C-terminal domain of CREPT and p15RS in recognizing RNA Pol II.
文摘第二类肽链释放因子eRF3(eukaryotic polypeptide release factor)是一种GTPase,它促进第一类肽链释放因子eRF1的释放活性,并与细胞周期调控、细胞骨架组装、细胞凋亡和肿瘤形成等过程相关。哺乳动物细胞中eRF3有两种——eRF3a和eRF3b,分别由GSPT1和GSPT2(G1 to S phase transition 1/2)基因编码。生存素(survivin)是迄今发现的最强有力的凋亡抑制因子,具有独特的结构和复杂的功能,不仅可以抑制细胞凋亡,还参与细胞有丝分裂、血管的生成等过程。eRF3和survivin都与细胞周期和细胞凋亡的调控相关。该实验室的前期研究表明,eRF3和survivin具有相互作用关系。该研究进一步对eRF3a进行截短突变,采用酵母双杂交和pull-down两种分析方法依次验证eRF3a(1-72aa)和eRF3a(1-36aa)与survivin的相互作用关系。结果表明,eRF3a(1-72aa)和eRF3a(1-36aa)均可以与survivin相互作用,由此确定eRF3a与survivin相互作用的最小结构域位于其N末端1-36aa之间,从而为进一步证实eRF3a的N端结构域与survivin协同作用参与细胞周期和细胞凋亡的调控提供了数据支持。
