TY - JOUR
T1 - Cryo-EM visualization of a viral internal ribosome entry site bound to human ribosomes
T2 - The IRES functions as an RNA-based translation factor
AU - Spahn, Christian M.T.
AU - Jan, Eric
AU - Mulder, Anke
AU - Grassucci, Robert A.
AU - Sarnow, Peter
AU - Frank, Joachim
N1 - Funding Information:
Supported in part by HHMI and NIH R037 GM29169, R01 GM55440, and P41 RR01219 (to J.F.); NSF DBI-9987844 (to A.M.); NIH (GM55979) (to P.S); DRG-1630 of the Damon Runyon Cancer Research Foundation (to E.J.); and the VolkswagenStiftung (to C.M.T.S.).
PY - 2004/8/20
Y1 - 2004/8/20
N2 - Internal initiation of protein synthesis in eukaryotes is accomplished by recruitment of ribosomes to structured internal ribosome entry sites (IRESs), which are located in certain viral and cellular messenger RNAs. An IRES element in cricket paralysis virus (CrPV) can directly assemble 80S ribosomes in the absence of canonical initiation factors and initiator tRNA. Here we present cryo-EM structures of the CrPV IRES bound to the human ribosomal 40S subunit and to the 80S ribosome. The CrPV IRES adopts a defined, elongate structure within the ribosomal intersubunit space and forms specific contacts with components of the ribosomal A, P, and E sites. Conformational changes in the ribosome as well as within the IRES itself show that CrPV IRES actively manipulates the ribosome. CrPV-like IRES elements seem to act as RNA-based translation factors.
AB - Internal initiation of protein synthesis in eukaryotes is accomplished by recruitment of ribosomes to structured internal ribosome entry sites (IRESs), which are located in certain viral and cellular messenger RNAs. An IRES element in cricket paralysis virus (CrPV) can directly assemble 80S ribosomes in the absence of canonical initiation factors and initiator tRNA. Here we present cryo-EM structures of the CrPV IRES bound to the human ribosomal 40S subunit and to the 80S ribosome. The CrPV IRES adopts a defined, elongate structure within the ribosomal intersubunit space and forms specific contacts with components of the ribosomal A, P, and E sites. Conformational changes in the ribosome as well as within the IRES itself show that CrPV IRES actively manipulates the ribosome. CrPV-like IRES elements seem to act as RNA-based translation factors.
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U2 - 10.1016/j.cell.2004.08.001
DO - 10.1016/j.cell.2004.08.001
M3 - Article
C2 - 15315759
AN - SCOPUS:4644247805
SN - 0092-8674
VL - 118
SP - 465
EP - 475
JO - Cell
JF - Cell
IS - 4
ER -