Release of Polypeptide Chain Initiation Factor IF-2 During Initiation Complex Formation

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1972 Dec 1

PMID 4566451

Citations 12

Authors

A H Lockwood

P Sarkar

U Maitra

Affiliations

Soon will be listed here.

Abstract

Polypeptide chain initiation factor IF-2 binds to 30S ribosomal subunits. This binding is enhanced by IF-1 and IF-3. During GTP-dependent formation of a 70S initiation complex, IF-2 is released from the ribosome. During 70S initiation complex formation dependent on the methylene analogue of GTP, GMPPCH(2)P, IF-2 is not released, but remains bound to the 70S ribosome. This result suggests that IF-2 release requires GTP hydrolysis. In agreement with this presumed requirement, IF-2 functions catalytically with GTP, but stoichiometrically with GMPPCH(2)P, in bringing about 70S initiation complex formation.

Citing Articles

Disparate Phenotypes Resulting from Mutations of a Single Histidine in Switch II of Translation Initiation Factor IF2.

Tomsic J, Smorlesi A, Caserta E, Giuliodori A, Pon C, Gualerzi C Int J Mol Sci. 2020; 21(3).

PMID: 31979156 PMC: 7037019. DOI: 10.3390/ijms21030735.

Directional transition from initiation to elongation in bacterial translation.

Goyal A, Belardinelli R, Maracci C, Milon P, Rodnina M Nucleic Acids Res. 2015; 43(22):10700-12.

PMID: 26338773 PMC: 4678851. DOI: 10.1093/nar/gkv869.

Single-molecule analysis of translational dynamics.

Petrov A, Chen J, OLeary S, Tsai A, Puglisi J Cold Spring Harb Perspect Biol. 2012; 4(9):a011551.

PMID: 22798542 PMC: 3428772. DOI: 10.1101/cshperspect.a011551.

Translation initiation without IF2-dependent GTP hydrolysis.

Fabbretti A, Brandi L, Milon P, Spurio R, Pon C, Gualerzi C Nucleic Acids Res. 2012; 40(16):7946-55.

PMID: 22723375 PMC: 3439930. DOI: 10.1093/nar/gks569.

Heterogeneous pathways and timing of factor departure during translation initiation.

Tsai A, Petrov A, Marshall R, Korlach J, Uemura S, Puglisi J Nature. 2012; 487(7407):390-3.

PMID: 22722848 PMC: 4465488. DOI: 10.1038/nature11172.

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