对大肠杆菌中表达蛋白质精氨酸甲基转移酶5的几个缺失突变体的活性研究.pdfVIP

维普资讯 II]I] WV~~V．pibb．ac．cn StudyonBiologicalActivityofVarious T1rruunnccaattiioonnssoofiHHuummaannPRMM T|l。5i。nE．．ccooli术 SUN Li-Tao ，ZHOU Zhong-W ei，XIEXiao-Dong BAO Shi-Lai” Q)DepartnventofLfieSciences，LanzhouUniversity,Lanzhou730000，China；KeyLabortaoryofMolecularandDevelopmentalBiolog? InstituteofGenetksandDevelopnventalBiolo~，TheChineseAcademyofSciences，Beijing100101，China) Abstract Proteinargininemethyltransferase5(PRMT5)hasbeenimplicatedasanimportantregulatorofmanycellularprocessesand signalingpathways，includingchromatinremodeling，RNA splicing，DNA transcription，andcellproliferation．Therefore，structuraland functionaIsutdiesonPRMT5arequiteimportant．ThefuIIlengthof MT5genewasclonedintovectorpGEX-41T_1 ． resultinginonly lowexpressionlevelsinEscherichiacol coli)．Here，itwasshowedthattheseveralN-terminalaminoacidsdeletionscouldresultin asing ificantincreaseintheamountofsolublefraction．whileoneofthem didnotaffecttheprotein．argininemethylrtansferaseactivity． Anditwasalsofoun dthattheN-terminall5aminoacidsregionofPRMT5maybeimportantforthecatalyticactiviyt． Keywords PRMT5，expression，purification，methyltransferasesactivity ProteinarginineN．methyltransferases(PRMTs) Recruitment of proteins methylated by PRM T5 is areeukaryoticenzymesthatcatalyzethemethylgroups involvedintheinductionoftheinterleukin一2genein transferring from S．adenosylmethionine (SAM) to m itogenactivatedJurkatT cellsandhumanperipheral arginineresiduesofnumerousPRM T subsrtates[， ． blood lymphocytes 2[2】．PRMT5 also exhibits the Theiractivities influencea wide range ofcellular methyltransferaseactivitytowardsmyelinbasicprotein processes，includingce