Macromolecular Mimicry in Translation Initiation: A Model for the Initiation Factor IF2 on the Ribosome

Moreno, Juan Manuel Palacios; Sørensen, H.; Mortensen, Karen Vibeke; Sperling‐Petersen, Hans Uffe

doi:10.1080/713803743

Cited by 15 publications

(9 citation statements)

References 54 publications

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“…IF-1 binds to the A site and interacts specifically with IF-2, while IF-3 acts as an antiassociation factor, keeping the large and small subunits apart prior to the correct association of the fMet-tRNA fMet anticodon to the P site. The hydrolysis of GTP on IF-2 and the subsequent dissociation of the IFs from the ribosome and the binding of the 50S subunit comprise the final initiation steps: the ribosome is now primed for elongation (6,147,187,239). The presence of IF-2 ⅐ GTP in the 30S initiation complex and GTP hydrolysis during 70S complex formation are essential for the initiation of protein biosynthesis.…”

Section: If-2 (Infb)mentioning

confidence: 99%

“…Upon peptide release, the ribosome-recycling factor (RRF) binds to the ribosomal A site. Next, EF-G translocates RRF to the P site, which results in the ejection of deacylated tRNA from the ribosome, ultimately leading to dissociation into mRNA, tRNA, and the ribosomal subunits ready for recycling (130,187). EF-G is the target of the antibacterial compound fusidic acid, which binds to EF-G and prevents the release of EF-G ⅐ GDP from the ribosome.…”

Section: Ef-g (Fusa)mentioning

confidence: 99%

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The Universally Conserved Prokaryotic GTPases

Verstraeten

Fauvart

Versées

et al. 2011

Microbiol Mol Biol Rev

186

251

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SUMMARY Members of the large superclass of P-loop GTPases share a core domain with a conserved three-dimensional structure. In eukaryotes, these proteins are implicated in various crucial cellular processes, including translation, membrane trafficking, cell cycle progression, and membrane signaling. As targets of mutation and toxins, GTPases are involved in the pathogenesis of cancer and infectious diseases. In prokaryotes also, it is hard to overestimate the importance of GTPases in cell physiology. Numerous papers have shed new light on the role of bacterial GTPases in cell cycle regulation, ribosome assembly, the stress response, and other cellular processes. Moreover, bacterial GTPases have been identified as high-potential drug targets. A key paper published over 2 decades ago stated that, “It may never again be possible to capture [GTPases] in a family portrait” (H. R. Bourne, D. A. Sanders, and F. McCormick, Nature 348 :125-132, 1990) and indeed, the last 20 years have seen a tremendous increase in publications on the subject. Sequence analysis identified 13 bacterial GTPases that are conserved in at least 75% of all bacterial species. We here provide an overview of these 13 protein subfamilies, covering their cellular functions as well as cellular localization and expression levels, three-dimensional structures, biochemical properties, and gene organization. Conserved roles in eukaryotic homologs will be discussed as well. A comprehensive overview summarizing current knowledge on prokaryotic GTPases will aid in further elucidating the function of these important proteins.

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Section: If-2 (Infb)mentioning

confidence: 99%

Section: Ef-g (Fusa)mentioning

confidence: 99%

The Universally Conserved Prokaryotic GTPases

Verstraeten

Fauvart

Versées

et al. 2011

Microbiol Mol Biol Rev

186

251

View full text Add to dashboard Cite

show abstract

“…Based on the alignments of sequences from bacterial, archaeal and eukaryal organisms, IF2 can be divided into a variable N-terminal part and a conserved C-terminal part (Moreno et al . 2000;Sørensen et al .…”

Section: Introductionmentioning

confidence: 99%

“…2001). We have proposed a six-domain structural model for E. coli IF2, in which the variable part corresponds to the N-terminal domains I, II and III, while the conserved part is the C-terminal domains IV, V and VI (Moreno et al . 2000;Mortensen et al .…”

Section: Introductionmentioning

confidence: 99%

Structural requirements of the mRNA for intracistronic translation initiation of the enterobacterial infB gene

et al. 2002

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Background : The gene infB encodes the prokaryotic translation initiation factor IF2, a central macromolecular component in the formation of the ribosomal 70S initiation complex. In Escherichia coli , infB encodes three forms of IF2: IF2 α α α α , IF2 β β β β and IF2 γ γ γ γ . The expression of IF2 β β β β and IF2 γ γ γ γ is a tandem translation from intact infB mRNA and not merely a translation of post-transcriptionally truncated mRNA. The molecular mechanism responsible for the ribosomal recognition of the two intracistronic translation initiation sites in E. coli infB is not well characterized.

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“…Initiation of protein biosynthesis is a universal process involving variable combinations and numbers of macromolecular amino acid and nucleotide-based components. A macromolecular core represented by the ribosomal subunits, including rRNAs and ribosomal proteins, initiator tRNA, and two translation initiation factors IF1/eIF1A and IF2/eIF5B, conserved throughout evolution, are essential for appropriate translation initiation (1)(2)(3).…”

Section: Introductionmentioning

confidence: 99%

Remarkable Conservation of Translation Initiation Factors: IF1/eIF1A and IF2/eIF5B are Universally Distributed Phylogenetic Markers

Sørensen

Hedegaard²,

Sperling‐Petersen³

et al. 2001

IUBMB Life

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Initiation of protein biosynthesis is an essential process occurring in cells throughout the three phylogenetic domains, Bacteria, Archaea, and Eucarya. IF1/eIF1A and IF2/eIF5B, two conserved translation initiation factors are involved in this important step of protein biosynthesis. The essentiality, universal distribution, conservation, and interspecies functional homology of both factors are a unique combination of properties ideal for molecular phylogenetic studies as demonstrated by the extensively compared SSU rRNAs. Here, we assess the use of IF1/eIF1A and IF2/eIF5B in universal and partial phylogenetic studies by comparison of sequence information from species within all three phylogenetic domains and among closely related strains of Haemophilus parainfluenzae. We conclude that the amino acid sequence of IF1/eIF1A-IF2/eIF5B is a universal phylogenetic marker and that the nucleotide sequence of the IF2/eIF5B G-domain is more credible than SSU rRNA for the construction of partial phylogenies among closely related species and strains. Because of these two application levels, IF1/eIF1A-IF2/eIF5B is a phylogenetic "dual level" marker.

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Macromolecular Mimicry in Translation Initiation: A Model for the Initiation Factor IF2 on the Ribosome

Cited by 15 publications

References 54 publications

The Universally Conserved Prokaryotic GTPases

The Universally Conserved Prokaryotic GTPases

Structural requirements of the mRNA for intracistronic translation initiation of the enterobacterial infB gene

Remarkable Conservation of Translation Initiation Factors: IF1/eIF1A and IF2/eIF5B are Universally Distributed Phylogenetic Markers

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