{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,22]],"date-time":"2025-10-22T02:52:28Z","timestamp":1761101548344},"reference-count":52,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2002,1,25]],"date-time":"2002-01-25T00:00:00Z","timestamp":1011916800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2002,3,6]]},"abstract":"<jats:p>Photoreactive derivatives of yeast tRNA<jats:sup>Phe<\/jats:sup> containing 2\u2010azidoadenosine at their 3\u2032 termini were used to trace the movement of tRNA across the 50S subunit during its transit from the P site to the E site of the 70S ribosome. When bound to the P site of poly(U)\u2010programmed ribosomes, deacylated tRNA<jats:sup>Phe<\/jats:sup>, Phe\u2010tRNA<jats:sup>Phe<\/jats:sup> and <jats:italic>N<\/jats:italic>\u2010acetyl\u2010Phe\u2010tRNA<jats:sup>Phe<\/jats:sup> probes labeled protein L27 and two main sites within domain V of the 23S RNA. In contrast, deacylated tRNA<jats:sup>Phe<\/jats:sup> bound to the E site in the presence of poly(U) labeled protein L33 and a single site within domain V of the 23S rRNA. In the absence of poly(U), the deacylated tRNA<jats:sup>Phe<\/jats:sup> probe also labeled protein L1. Cross\u2010linking experiments with vacant 70S ribosomes revealed that deacylated tRNA enters the P site through the E site, progressively labeling proteins L1, L33 and, finally, L27. In the course of this process, tRNA passes through the intermediate P\/E binding state. These findings suggest that the transit of tRNA from the P site to the E site involves the same interactions, but in reverse order. Moreover, our results indicate that the final release of deacylated tRNA from the ribosome is mediated by the F site, for which protein L1 serves as a marker. The results also show that the precise placement of the acceptor end of tRNA on the 50S subunit at the P and E sites is influenced in subtle ways both by the presence of aminoacyl or peptidyl moieties and, more surprisingly, by the environment of the anticodon on the 30S subunit.<\/jats:p>","DOI":"10.1016\/s0014-5793(02)02302-5","type":"journal-article","created":{"date-parts":[[2002,10,14]],"date-time":"2002-10-14T15:56:01Z","timestamp":1034610961000},"page":"60-66","source":"Crossref","is-referenced-by-count":16,"title":["Transit of tRNA through the <i>Escherichia coli<\/i> ribosome: cross\u2010linking of the 3\u2032 end of tRNA to ribosomal proteins at the P and E sites"],"prefix":"10.1002","volume":"514","author":[{"given":"Stanislav V","family":"Kirillov","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jacek","family":"Wower","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephen S","family":"Hixson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert A","family":"Zimmermann","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2002,1,25]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1139\/o95-111"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(97)00261-5"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M005031200"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/0167-4781(94)90212-7"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00321a066"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1080\/07391102.1986.10506345"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(88)90203-3"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.7124\/bc.000044"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1993.tb05694.x"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1060089"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(01)00435-4"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.271.5251.1000"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81854-1"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1038\/342142a0"},{"key":"e_1_2_6_16_1","unstructured":"Noller H.F. 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