Backbone 1H, 13C, and 15N assignments of the ribosome recycling factor from Thermus thermophillus.
Backbone 1H, 13C, and 15N assignments of the ribosome recycling factor from Thermus thermophillus.
复制标题
嗜热栖热菌核糖体循环因子的主链 1H、13C 和 15N 分配。
DOI：
10.1023/a:1020660725244
复制
发表时间：
2002
影响因子：
2.7
通讯作者：
Alam,StevenL
中科院分区：
文献类型：
--
作者：
Blake,BKelly;Ito,Koichi;Nakamura,Yoshikazu;Alam,StevenL
Termination of protein synthesis and the release of polypeptide products are signaled by the presence of a stop-codon in the ribosomal A-site. In Eubacteria, release factors (RF1, RF2 and RF3) recognize the stopcodon, trigger peptidyl-tRNA hydrolysis and peptide release, and dissociate from the ribosome (Nakamura et al., 2000). Following termination the ribosome is left in a ‘post-termination’state composed of the 70S ribosome, the RNA message, the final P-site deacylated tRNA and an empty A-site. Ribosomal release factor (RRF) orchestrates the disassembly of the posttermination complex (Hirokawa et al., 2002; Ito et al., 2002; Janosi et al., 1996). 70S or 50S dissociation promotes a ‘recycling’of the 30S and 50S subunits allowing translation to initiate on other RNA-messages; requirements for cell growth and efficient protein synthesis. Structures of ribosome recycling factors (Kim et al., 2000; Selmer et al., 1999; Toyoda et al., 2000) indicate RRF proteins adopt an L-shape consisting of a three-helix coil and a β/α/β sandwich separated by two loops. A similar shape to tRNA suggests RRF functions through tRNA mimicry. Ribosome recycling proteins are found only in prokaryotes and their vestiges (chloroplasts and mitochondria), making ribosome recycling an ideal anti-microbial target. Although structures of RRF are known, little is known about structural features responsible for the recycling action. Genetic studies suggest that ribosome recycling is dependent upon the structural or dynamic properties of the linker (or ‘hinge’regions) between the two domains (Toyoda et al., 2000). Here we report backbone 1H, 15N and 13C resonance assignments for
