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	Structural basis for the recognition of RNA polymerase II C-terminal domain by CREPT and p15RS
	MEI KunRong ; JIN Zhe ; REN FangLi ; WANG YinYing ; CHANG ZhiJie ; WANG XinQuan ; MEI KunRong ; JIN Zhe ; REN FangLi ; WANG YinYing ; CHANG ZhiJie ; WANG XinQuan
	2016-03-30 ; 2016-03-30
关键词	CREPT p15RS structure RPR domain C-terminal domain RNA Pol II R730.2
其他题名	Structural basis for the recognition of RNA polymerase II C-terminal domain by CREPT and p15RS
中文摘要	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.; 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.
语种	英语 ; 英语
内容类型	期刊论文
源URL	[http://ir.lib.tsinghua.edu.cn/ir/item.do?handle=123456789/148499]
专题	清华大学
推荐引用方式 GB/T 7714	MEI KunRong,JIN Zhe,REN FangLi,et al. Structural basis for the recognition of RNA polymerase II C-terminal domain by CREPT and p15RS[J],2016, 2016.
APA	MEI KunRong.,JIN Zhe.,REN FangLi.,WANG YinYing.,CHANG ZhiJie.,...&WANG XinQuan.(2016).Structural basis for the recognition of RNA polymerase II C-terminal domain by CREPT and p15RS..
MLA	MEI KunRong,et al."Structural basis for the recognition of RNA polymerase II C-terminal domain by CREPT and p15RS".(2016).

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