title: Three tRNA binding sites in rabbit liver ribosomes and role of the intrinsic ATPase in 80S ribosomes from higher eukaryotes.
abstract: Three tRNA binding sites have been found in organisms of all domains (former kingdoms) with only one exception: Four binding sites have been reported for cytoplasmic 80S ribosomes from rabbit liver. Therefore, the issue was reconsidered, and the data revealed that rabbit liver ribosomes contain three tRNA binding sites, underlining the universal character of this ribosomal feature. Furthermore, a first analysis of the role of the ribosome intrinsic ATPase was performed. This ATPase is found in ribosomes of higher eukarya but not in lower eukarya such as yeast or ribosomes of the domains archea and bacteria. The results suggest that the intrinsic ATPase fulfills the same function as the essential third elongation factor EF-3, an ATPase in higher fungi (yeast etc.), that facilitates the release of the deacylated tRNA from the E site.
authors.affiliation: Institute of Molecular Biology & Genetics of the National Academy of Sciences of Ukraine, Kiev, Ukraine.
authors.forename: A V
authors.initials: AV
authors.lastname: El'skaya
authors.forename: G V
authors.initials: GV
authors.lastname: Ovcharenko
authors.forename: S S
authors.initials: SS
authors.lastname: Palchevskii
authors.forename: Z M
authors.initials: ZM
authors.lastname: Petrushenko
authors.forename: F J
authors.initials: FJ
authors.lastname: Triana-Alonso
authors.forename: K H
authors.initials: KH
authors.lastname: Nierhaus
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D008099:Liver / Q000737:chemistry / Q000378:metabolism*; D008274:Magnesium / Q000494:pharmacology; D009711:Nucleotides / Q000494:pharmacology; D010452:Peptide Biosynthesis; D010455:Peptides / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism*; D012360:RNA, Transfer, Phe / Q000378:metabolism; D011817:Rabbits; D012269:Ribosomal Proteins / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry / Q000201:enzymology / Q000378:metabolism*; D013096:Spermine / Q000494:pharmacology
chemical_list: D009711:Nucleotides; D010455:Peptides; D012333:RNA, Messenger; D012360:RNA, Transfer, Phe; D012269:Ribosomal Proteins; C039913:ribosomal protein S80; D013096:Spermine; C012001:polyphenylalanine; D000255:Adenosine Triphosphate; D012343:RNA, Transfer; D000251:Adenosine Triphosphatases; D008274:Magnesium