Abstract：
:Ribosomes catalyze the formation of peptide bonds between aminoacyl esters of transfer RNAs within a catalytic center composed of ribosomal RNA only. Here we show that the reaction of P-site formylmethionine (fMet)-tRNA(fMet) with a modified A-site tRNA substrate, Phelac-tRNA(Phe), in which the nucleophilic amino group is replaced with a hydroxyl group, does not show the pH dependence observed with small substrate analogs such as puromycin and hydroxypuromycin. This indicates that acid-base catalysis by ribosomal residues is not important in the reaction with the full-size substrate. Rather, the ribosome catalyzes peptide bond formation by positioning the tRNAs, or their 3' termini, through interactions with rRNA that induce and/or stabilize a pH-insensitive conformation of the active site and provide a preorganized environment facilitating the reaction. The rate of peptide bond formation with unmodified Phe-tRNA(Phe) is estimated to be >300 s(-1).
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Bieling P,Beringer M,Adio S,Rodnina MVdoi
10.1038/nsmb1091subject
Has Abstractpub_date
2006-05-01 00:00:00pages
423-8issue
5eissn
1545-9993issn
1545-9985pii
nsmb1091journal_volume
13pub_type
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