z-logo
open-access-imgOpen Access
Specific, efficient, and selective inhibition of prokaryotic translation initiation by a novel peptide antibiotic
Author(s) -
Letizia Brandi,
Attilio Fabbretti,
Anna La Teana,
Monica Abbondi,
Daniele Losi,
Stefano Donadio,
Claudio O. Gualerzi
Publication year - 2005
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0507740102
Subject(s) - ribosome , protein biosynthesis , initiation factor , biology , peptidyl transferase , eukaryotic translation , 30s , eukaryotic initiation factor , translation (biology) , in vitro , tetrapeptide , ribosomal rna , streptomyces , biochemistry , protein subunit , internal ribosome entry site , peptide , rna , bacteria , messenger rna , gene , genetics
Many known antibiotics target the translational apparatus, but none of them can selectively inhibit initiation of protein synthesis and/or is prokaryotic-specific. This article describes the properties of GE81112, an effective and prokaryotic-specific initiation inhibitor. GE81112 is a natural tetrapeptide produced by a Streptomyces sp. identified by an in vitro high-throughput screening test developed to find inhibitors of the prokaryotic translational apparatus preferentially acting on steps other than elongation. In vivo GE81112 inhibits protein synthesis but not other cell functions such as DNA duplication, transcription, and cell wall synthesis. In vitro GE81112 was found to target the 30S ribosomal subunit and to interfere with both coded and noncoded P-site binding of fMet-tRNA, thereby selectively inhibiting formation of the 30S initiation complex.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom