Initiation and Inhibition of Protein Biosynthesis - Studies at High Resolution

Title: Initiation and Inhibition of Protein Biosynthesis - Studies at High Resolution

Volume: 3 Issue: 1

Author(s): Raz Zarivach, Anat Bashan, Frank Schluenzen, Joerg Harms, Marta Pioletti, Francois Franceschi and Ada Yonath

Affiliation:

Keywords: Inhibition, Protein Biosynthesis, Thermus thermophilus, conformation mobility, edeine, tetracycline

Abstract: Analysis of the high resolution structure of the small subunit from Thermus thermophilus shed light on its inherent conformational variability and indicated an interconnected network of features allowing concerted movements during translocation. It also showed that conformational rearrangements may be involved in subunit association and that a latch-like movement guarantees processivity and ensures maximized fidelity. Conformational mobility is associated with the binding and the anti association function of initiation factor 3, and antibiotics interfering with prevent the initiation of the biosynthetic process. Proteins stabilize the structure mainly by their long basic extensions that penetrate into the ribosomal RNA. When pointing into the solution, these extensions may have functional roles in binding of non-ribosomal factors participating in the process of protein biosynthesis. In addition, although the decoding center is formed of RNA, proteins seem to serve ancillary functions such as stabi lizing ist required conformation and assisting the directionality of the translocation.

Cite this article as:

Zarivach Raz, Bashan Anat, Schluenzen Frank, Harms Joerg, Pioletti Marta, Franceschi Francois and Yonath Ada, Initiation and Inhibition of Protein Biosynthesis - Studies at High Resolution, Current Protein & Peptide Science 2002; 3 (1) . https://dx.doi.org/10.2174/1389203023380800

DOI https://dx.doi.org/10.2174/1389203023380800	Print ISSN 1389-2037
Publisher Name Bentham Science Publisher	Online ISSN 1875-5550