Phenylboric acids — a new group of peptidyl transferase inhibitors

Černá, J.; Rychlík, Ivan

doi:10.1016/0014-5793(80)80285-7

Cited by 15 publications

References 21 publications

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Das 3′‐Ende der tRNA und seine Rolle bei der Proteinbiosynthese

Chládek

Sprinzl

1985

Angewandte Chemie

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Wahrend der Proteinbiosynthese wechselwirken das 3'-Ende der Aminoacyl-tRNA (aatRN A) und der Peptidyl-tRNA spezifisch rnit Makromolekiilen des Proteinbiosynthese-Apparats. Das 3'-Ende der tRNAs besteht aus einem invarianten C-C-A-Einzelstrang. Die Wechselwirkung des 3'-Endes der aa-tRNA mit dem Elongationsfaktor (EF) ist wichtig fiir die Bildung des aa-tRNA . EF-Tu.GTP-Komplexes und, nachdem dieser Komplex an das Ribosom gebunden ist, fur die GTP-Hydrolyse. Diesem Vorgang folgt die spezifische Bindung des 3'-Endes der Aminoacyl-tRNA an die Acceptorstelle der ribosomalen Peptidyltransferase. In diesem Aufsatz wird ein Modell vorgestellt, nach welchem die C-C-Nucleotide des 3'-Endes der Aminoacyl-tRNA mit einer spezifischen G-G-Sequenz der ribosomalen 23s-RNA Watson-Crick-Basenpaare bilden. Ahnlich bindet die Peptidyl-tRNA mit ihrem 3'-Ende an die komplementare Sequenz der ribosomalen 23s-RNA. Wir schlagen vor, da13 die Bildung der Peptidbindung zwischen den beiden tRNAs durch einen Bereich der 23s-RNA katalysiert wird, der sich in der Nahe des 3'-Endes der Aminoacyl-und der Peptidyl-tRNA befindet. An der Bindung der 3'-Enden der beiden tRNAs sowie an der Katalyse sind zwei Schleifen der 23s-RNA beteiligt, welche durch Faltung in unmittelbare Nachbarschaft gebracht werden k6nnen. Das vorgeschlagene Modell setzt eine dynamische Struktur der ribosomalen RNA voraus, die durch Wechselwirkungen rnit Elongationsfaktoren und ribosomalen Proteinen funktionell verandert und gesteuert wird.

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Das 3′‐Ende der tRNA und seine Rolle bei der Proteinbiosynthese

Chládek

Sprinzl

1985

Angewandte Chemie

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The 3′‐End of tRNA and Its Role in Protein Biosynthesis

Chládek

Sprinzl

1985

Angew. Chem. Int. Ed. Engl.

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In the course of protein biosynthesis, the 3'-ends of aminoacyl-tRNA (aa-tRNA) and peptidyl-t RNA specifically interact with macromolecules of the protein biosynthesis machinery. The 3'-end of tRNA consists of an invariant C-C-A single strand. Interaction of the aminoacyl-tRNA 3'-end with elongation factor Tu (EF-Tu) containing bound GTP is necessary for the formation of the aa-tRNA. EF-TU . GTP complex and, after the complex binds to the ribosome, for the GTP hydrolysis. This process is followed by the specific binding of the aminoacyl-tRNA 3'-end to the aminoacyl (A) site of the ribosome. In this review, a model is proposed that involves Watson-Crick base pairing of the C-C sequence of the aminoacyltRNA 3'-end with a specific G-G sequence of the ribosomal 23s RNA. Similarly, peptidyltRNA binds with its 3'-end to the peptidyl (P) site of the ribosome. This binding may also involve Watson-Crick base pairing of the C-C-A sequence with a complementary sequence of 23s RNA. It is proposed that peptide bond formation is catalyzed by a functional site of the 23s RNA located near the 3'-ends of aminoacyl-tRNA and peptidyl-tRNA. A model is suggested in which two loops of the 23s RNA, brought into close proximity via folding, are involved both in binding the 3'-ends of the tRNAs and in catalyzing peptide bond formation. This model presumes a dynamic structure for ribosomal RNA, which is modulated by interaction with elongation factors and ribosomal proteins.

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Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity.

Schulze¹,

Nierhaus²

1982

The EMBO Journal

140

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A new approach is described to gain further information concerning the ribosomal components involved in the peptidyltransferase (PTF) activity exerted by Escherichia coli 50S subunits. A particle is reconstituted from highly purified proteins and RNA under modified incubation conditions. This particle contains only 16 out of the 34 distinct components constituting the native subunit, and yet still exhibits significant PTF activity. Single omission tests at the level of this “minimal ribosomal particle” indicate the limits set on a further reduction of the components, and in particular reveal that protein L18 can be excluded from the set of proteins which are essential for PTF activity, thus leaving L2, L3, L4, L15, and L16 as primary candidates for this function. 5S RNA is not needed for PTF activity of the “minimal ribosomal particle”. Furthermore, a buffer condition is described which drastically improves the stability of total protein preparations and facilitates the isolation of individual proteins.

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Phenylboric acids — a new group of peptidyl transferase inhibitors

Cited by 15 publications

References 21 publications

Das 3′‐Ende der tRNA und seine Rolle bei der Proteinbiosynthese

Das 3′‐Ende der tRNA und seine Rolle bei der Proteinbiosynthese

The 3′‐End of tRNA and Its Role in Protein Biosynthesis

Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity.

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