ASSEMBLY OF THE 68-KD AND 72-KD PROTEINS OF SIGNAL RECOGNITION PARTICLE WITH 7S RNA

被引:39
作者
LUTCKE, H
PREHN, S
ASHFORD, AJ
REMUS, M
FRANK, R
DOBBERSTEIN, B
机构
[1] EUROPEAN MOLEC BIOL LAB, CELL BIOL PROGRAMME, W-6900 HEIDELBERG, GERMANY
[2] HUMBOLDT UNIV BERLIN, INST BIOCHEM, O-1086 BERLIN, GERMANY
关键词
D O I
10.1083/jcb.121.5.977
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Signal recognition particle (SRP), the cytoplasmic ribonucleoprotein particle that mediates the targeting of proteins to the ER, consists of a 7S RNA and six different proteins. The 68- (SRP68) and 72- (SRP72) kD proteins of SRP are bound to the 7S RNA of SRP as a heterodimeric complex (SRP68/72). Here we describe the primary structure of SRP72 and the assembly of SRP68, SRP72 and 7S RNA into a ribonucleoprotein particle. The amino acid sequence deduced from the cDNA of SRP72 reveals a basic protein of 671 amino acids which shares no sequence similarity with any protein in the sequence data libraries. Assembly of SRP72 into a ribonucleoprotein particle required the presence of 7S RNA and SRP68. In contrast, SRP68 alone specifically bound to 7S RNA. SRP68 contacts the 7S RNA via its NH2-terminal half while COOH-terminal portions of SRP68 and SRP72 are in contact with each other in SRP. SRP68 thus serves as a link between 7S RNA and SRP72. As a large NH2-terminal domain of SRP72 is exposed on SRP it may be a site of contact to other molecules involved in the SRP cycle between the ribosome and the ER membrane.
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收藏
页码:977 / 985
页数:9
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