期刊
SCIENCE
卷 340, 期 6140, 页码 1543-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1236086
关键词
-
资金
- NIH [GM-17129, GM-59140, Y1-CO-1020, Y1-GM-1104, GM-105404, P41-GM-103393]
Translocation of messenger and transfer RNA (mRNA and tRNA) through the ribosome is a crucial step in protein synthesis, whose mechanism is not yet understood. The crystal structures of three Thermus ribosome-tRNA-mRNA-EF-G complexes trapped with beta,gamma-imidoguanosine 5'-triphosphate (GDPNP) or fusidic acid reveal conformational changes occurring during intermediate states of translocation, including large-scale rotation of the 30S subunit head and body. In all complexes, the tRNA acceptor ends occupy the 50S subunit E site, while their anticodon stem loops move with the head of the 30S subunit to positions between the P and E sites, forming chimeric intermediate states. Two universally conserved bases of 16S ribosomal RNA that intercalate between bases of the mRNA may act as pawls of a translocational ratchet. These findings provide new insights into the molecular mechanism of ribosomal translocation.
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