The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli

Patricia Julián, Pohl Milon, Xabier Agirrezabala, Gorka Lasso, David Gil, Marina V. Rodnina, Mikel Valle

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

Formation of the 30S initiation complex (30S IC) is an important checkpoint in regulation of gene expression. The selection of mRNA, correct start codon, and the initiator fMet-tRNA fMet requires the presence of three initiation factors (IF1, IF2, IF3) of which IF3 and IF1 control the fidelity of the process, while IF2 recruits fMet-tRNA fMet. Here we present a cryo-EM reconstruction of the complete 30S IC, containing mRNA, fMet-tRNA fMet, IF1, IF2, and IF3. In the 30S IC, IF2 contacts IF1, the 30S subunit shoulder, and the CCA end of fMet-tRNA fMet, which occupies a novel P/I position (P/I1). The N-terminal domain of IF3 contacts the tRNA, whereas the C-terminal domain is bound to the platform of the 30S subunit. Binding of initiation factors and fMet-tRNA fMet induces a rotation of the head relative to the body of the 30S subunit, which is likely to prevail through 50S subunit joining until GTP hydrolysis and dissociation of IF2 take place. The structure provides insights into the mechanism of mRNA selection during translation initiation.

Original languageEnglish (US)
Article numbere1001095
JournalPLoS biology
Volume9
Issue number7
DOIs
StatePublished - Jul 1 2011
Externally publishedYes

Fingerprint

start codon
gene expression regulation
shoulders
Escherichia coli
translation (genetics)
hydrolysis
Peptide Initiation Factors
Messenger RNA
RNA, Transfer, Met
Initiator Codon
Gene Expression Regulation
Transfer RNA
Guanosine Triphosphate
Gene expression
Joining
Hydrolysis
Head
fMet-tRNA(fMet)

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Agricultural and Biological Sciences(all)

Cite this

Julián, P., Milon, P., Agirrezabala, X., Lasso, G., Gil, D., Rodnina, M. V., & Valle, M. (2011). The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli. PLoS biology, 9(7), [e1001095]. https://doi.org/10.1371/journal.pbio.1001095

The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli. / Julián, Patricia; Milon, Pohl; Agirrezabala, Xabier; Lasso, Gorka; Gil, David; Rodnina, Marina V.; Valle, Mikel.

In: PLoS biology, Vol. 9, No. 7, e1001095, 01.07.2011.

Research output: Contribution to journalArticle

Julián, P, Milon, P, Agirrezabala, X, Lasso, G, Gil, D, Rodnina, MV & Valle, M 2011, 'The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli', PLoS biology, vol. 9, no. 7, e1001095. https://doi.org/10.1371/journal.pbio.1001095
Julián, Patricia ; Milon, Pohl ; Agirrezabala, Xabier ; Lasso, Gorka ; Gil, David ; Rodnina, Marina V. ; Valle, Mikel. / The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli. In: PLoS biology. 2011 ; Vol. 9, No. 7.
@article{1db02e09685e4db6b422ecbd4a163205,
title = "The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli",
abstract = "Formation of the 30S initiation complex (30S IC) is an important checkpoint in regulation of gene expression. The selection of mRNA, correct start codon, and the initiator fMet-tRNA fMet requires the presence of three initiation factors (IF1, IF2, IF3) of which IF3 and IF1 control the fidelity of the process, while IF2 recruits fMet-tRNA fMet. Here we present a cryo-EM reconstruction of the complete 30S IC, containing mRNA, fMet-tRNA fMet, IF1, IF2, and IF3. In the 30S IC, IF2 contacts IF1, the 30S subunit shoulder, and the CCA end of fMet-tRNA fMet, which occupies a novel P/I position (P/I1). The N-terminal domain of IF3 contacts the tRNA, whereas the C-terminal domain is bound to the platform of the 30S subunit. Binding of initiation factors and fMet-tRNA fMet induces a rotation of the head relative to the body of the 30S subunit, which is likely to prevail through 50S subunit joining until GTP hydrolysis and dissociation of IF2 take place. The structure provides insights into the mechanism of mRNA selection during translation initiation.",
author = "Patricia Juli{\'a}n and Pohl Milon and Xabier Agirrezabala and Gorka Lasso and David Gil and Rodnina, {Marina V.} and Mikel Valle",
year = "2011",
month = "7",
day = "1",
doi = "10.1371/journal.pbio.1001095",
language = "English (US)",
volume = "9",
journal = "PLoS Biology",
issn = "1544-9173",
publisher = "Public Library of Science",
number = "7",

}

TY - JOUR

T1 - The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli

AU - Julián, Patricia

AU - Milon, Pohl

AU - Agirrezabala, Xabier

AU - Lasso, Gorka

AU - Gil, David

AU - Rodnina, Marina V.

AU - Valle, Mikel

PY - 2011/7/1

Y1 - 2011/7/1

N2 - Formation of the 30S initiation complex (30S IC) is an important checkpoint in regulation of gene expression. The selection of mRNA, correct start codon, and the initiator fMet-tRNA fMet requires the presence of three initiation factors (IF1, IF2, IF3) of which IF3 and IF1 control the fidelity of the process, while IF2 recruits fMet-tRNA fMet. Here we present a cryo-EM reconstruction of the complete 30S IC, containing mRNA, fMet-tRNA fMet, IF1, IF2, and IF3. In the 30S IC, IF2 contacts IF1, the 30S subunit shoulder, and the CCA end of fMet-tRNA fMet, which occupies a novel P/I position (P/I1). The N-terminal domain of IF3 contacts the tRNA, whereas the C-terminal domain is bound to the platform of the 30S subunit. Binding of initiation factors and fMet-tRNA fMet induces a rotation of the head relative to the body of the 30S subunit, which is likely to prevail through 50S subunit joining until GTP hydrolysis and dissociation of IF2 take place. The structure provides insights into the mechanism of mRNA selection during translation initiation.

AB - Formation of the 30S initiation complex (30S IC) is an important checkpoint in regulation of gene expression. The selection of mRNA, correct start codon, and the initiator fMet-tRNA fMet requires the presence of three initiation factors (IF1, IF2, IF3) of which IF3 and IF1 control the fidelity of the process, while IF2 recruits fMet-tRNA fMet. Here we present a cryo-EM reconstruction of the complete 30S IC, containing mRNA, fMet-tRNA fMet, IF1, IF2, and IF3. In the 30S IC, IF2 contacts IF1, the 30S subunit shoulder, and the CCA end of fMet-tRNA fMet, which occupies a novel P/I position (P/I1). The N-terminal domain of IF3 contacts the tRNA, whereas the C-terminal domain is bound to the platform of the 30S subunit. Binding of initiation factors and fMet-tRNA fMet induces a rotation of the head relative to the body of the 30S subunit, which is likely to prevail through 50S subunit joining until GTP hydrolysis and dissociation of IF2 take place. The structure provides insights into the mechanism of mRNA selection during translation initiation.

UR - http://www.scopus.com/inward/record.url?scp=79960917084&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79960917084&partnerID=8YFLogxK

U2 - 10.1371/journal.pbio.1001095

DO - 10.1371/journal.pbio.1001095

M3 - Article

C2 - 21750663

AN - SCOPUS:79960917084

VL - 9

JO - PLoS Biology

JF - PLoS Biology

SN - 1544-9173

IS - 7

M1 - e1001095

ER -