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J. Biol. Chem., Vol. 275, Issue 48, 37887-37894, December 1, 2000
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From the When bound to Escherichia coli
ribosomes and irradiated with near-UV light, various derivatives of
yeast tRNAPhe containing 2-azidoadenosine at the 3'
terminus form cross-links to 23 S rRNA and 50 S subunit proteins
in a site-dependent manner. A and P site-bound tRNAs, whose
3' termini reside in the peptidyl transferase center, label primarily
nucleotides U2506 and U2585 and protein L27. In contrast, E site-bound
tRNA labels nucleotide C2422 and protein L33. The cross-linking
patterns confirm the topographical separation of the peptidyl
transferase center from the E site domain. The relative amounts of
label incorporated into the universally conserved residues U2506 and
U2585 depend on the occupancy of the A and P sites by different tRNA
ligands and indicates that these nucleotides play a pivotal role in
peptide transfer. In particular, the 3'-adenosine of the peptidyl-tRNA analogue, AcPhe-tRNAPhe, remains in close contact with
U2506 regardless of whether its anticodon is located in the A site or P
site. Our findings, therefore, modify and extend the hybrid state model
of tRNA-ribosome interaction. We show that the 3'-end of the deacylated
tRNA that is formed after transpeptidation does not immediately
progress to the E site but remains temporarily in the peptidyl
transferase center. In addition, we demonstrate that the E site,
defined by the labeling of nucleotide C2422 and protein L33, represents
an intermediate state of binding that precedes the entry of deacylated
tRNA into the F (final) site from which it dissociates into the cytoplasm.
Transit of tRNA through the Escherichia coli
Ribosome
CROSS-LINKING OF THE 3' END OF tRNA TO SPECIFIC NUCLEOTIDES OF
THE 23 S RIBOSOMAL RNA AT THE A, P, AND E SITES*
§¶,
,§,, Department of Animal and Dairy Sciences,
Program in Cell and Molecular Biosciences, Auburn University, Auburn,
Alabama 36849-5415 and the Departments of § Biochemistry & Molecular Biology and ** Chemistry, University of Massachusetts,
Amherst, Massachusetts 01003
*
This research was supported by National Science Foundation
Grant MCB948732 and National Institutes of Health (NIH) Grant GM58267 (to J. W.) and by NIH Grant GM22807 (to R. A. Z.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Permanent address: Petersburg Nuclear Physics Institute,
Russian Academy of Sciences, Gatchina 188350, Leningrad Region, Russia.
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