Subtitle:

Role of RNA backbone groups for ribosomal catalysis

Publisher:

Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS

Type of object:

Journal/Article

Abstract:

The ribosomal peptidyl transferase ribozyme resides in the large ribosomal subunit and catalyzes the two principal chemical reactions of protein synthesis, peptide bond formation and peptidyl-tRNA hydrolysis. With the presentations of atomic structures of the large ribosomal subunit, the questions how an RNA active site can catalyze these chemical reactions gained a new level of molecular significance. The peptidyl transferase center represents the most intense accumulation of universally conserved ribosomal RNA nucleotides in the entire ribosome. Thus, it came as a surprise that recent findings revealed that the nucleobase identities of active site residues are actually not critical for catalysis. Instead RNA backbone groups have been identified as key players in transpeptidation and peptide release. While the ribose 2’-OH of the 23S rRNA residue A2451 plays an important role in peptidyl transfer, its contribution to peptidyl-tRNA hydrolysis is only minor. On the other hand, the ribose 2’-OH of the terminal adenosine of P-site bound tRNA seems to play equally crucial roles in peptide bond formation and tRNA hydrolysis. While it seems that details of ribosome-catalyzed peptidyl-tRNA hydrolysis are just emerging, our molecular insights into transpeptidation are already very advanced. It has been realized that an intricate interaction between the ribose 2’-OH groups of 23S rRNA residue A2451 and tRNA nucleotide A76 is crucial for proton shuttling that is required for efficient amide bond synthesis.

Relation:

Biotechnologia, vol.84, 1 (2009)-.

Volume:

84

Issue:

1

Start page:

65

End page:

80

Detailed Resource Type:

Article

Format:

application/pdf

Resource Identifier:

0860-7796 ; oai:rcin.org.pl:73112 ; IChB B-79

Source:

Library of Institute of Bioorganic Chemistry PAS

Language:

pol

Language of abstract:

eng

Temporal coverage:

2009

Rights:

Creative Commons Attribution BY-SA 4.0 license

Terms of use:

Copyright-protected material. [CC BY-SA 4.0] May be used within the scope specified in Creative Commons Attribution BY-SA 4.0 license, full text available at:

Digitizing institution:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Original in:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Projects co-financed by:

Operational Program Digital Poland, 2014-2020, Measure 2.3: Digital accessibility and usefulness of public sector information; funds from the European Regional Development Fund and national co-financing from the state budget.

Access:

Open