Structure, function and evolution of the signal recognition particle

被引:119
作者
Nagai, K
Oubridge, C
Kuglstatter, A
Menichelli, E
Isel, C
Jovine, L
机构
[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England
[2] Mt Sinai Sch Med, Brookdale Dept Mol Cell & Dev Biol, New York, NY 10029 USA
关键词
membrane targeting; ribosome nascent chain; signal recognition particle; translocon;
D O I
10.1093/emboj/cdg337
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The signal recognition particle (SRP) is a ribonucleoprotein particle essential for the targeting of signal peptide-bearing proteins to the prokaryotic plasma membrane or the eukaryotic endoplasmic reticulum membrane for secretion or membrane insertion. SRP binds to the signal peptide emerging from the exit site of the ribosome and forms a ribosome nascent chain (RNC)-SRP complex. The RNC-SRP complex then docks in a GTP-dependent manner with a membrane-anchored SRP receptor and the protein is translocated across or integrated into the membrane through a channel called the translocon. Recently considerable progress has been made in understanding the architecture and function of SRP.
引用
收藏
页码:3479 / 3485
页数:7
相关论文
共 53 条
[1]   The ribosome regulates the GTPase of the β-subunit of the signal recognition particle receptor [J].
Bacher, G ;
Pool, M ;
Dobberstein, B .
JOURNAL OF CELL BIOLOGY, 1999, 146 (04) :723-730
[2]   Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting [J].
Bacher, G ;
Lutcke, H ;
Jungnickel, B ;
Rapoport, TA ;
Dobberstein, B .
NATURE, 1996, 381 (6579) :248-251
[3]   Crystal structure of the ribonucleoprotein core of the signal recognition particle [J].
Batey, RT ;
Rambo, RP ;
Lucast, L ;
Rha, B ;
Doudna, JA .
SCIENCE, 2000, 287 (5456) :1232-+
[4]   Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle [J].
Batey, RT ;
Sagar, MB ;
Doudna, JA .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 307 (01) :229-246
[5]   Architecture of the protein-conducting channel associated with the translating 80S ribosome [J].
Beckmann, R ;
Spahn, CMT ;
Eswar, N ;
Helmers, J ;
Penczek, PA ;
Sali, A ;
Frank, J ;
Blobel, G .
CELL, 2001, 107 (03) :361-372
[6]   Assembly of archaeal signal recognition particle from recombinant components [J].
Bhuiyan, SH ;
Gowda, K ;
Hotokezaka, H ;
Zwieb, C .
NUCLEIC ACIDS RESEARCH, 2000, 28 (06) :1365-1373
[7]   The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14 [J].
Birse, DEA ;
Kapp, U ;
Strub, K ;
Cusack, S ;
Aberg, A .
EMBO JOURNAL, 1997, 16 (13) :3757-3766
[8]   Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 Å resolution:: Evidence for the mechanism of signal peptide binding [J].
Clemons, WM ;
Gowda, K ;
Black, SD ;
Zwieb, C ;
Ramakrishnan, V .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 292 (03) :697-705
[9]   Role of SRP19 in assembly of the Archaeoglobus fulgidus signal recognition particle [J].
Diener, JL ;
Wilson, C .
BIOCHEMISTRY, 2000, 39 (42) :12862-12874
[10]   A universal mode of helix packing in RNA [J].
Doherty, EA ;
Batey, RT ;
Masquida, B ;
Doudna, JA .
NATURE STRUCTURAL BIOLOGY, 2001, 8 (04) :339-343