Evidence map›Paper›PMID 28204695›Full record

ArticleNucleic acids research2017

Two highly conserved features of bacterial initiator tRNAs license them to pass through distinct checkpoints in translation initiation.

Sunil Shetty, Riyaz A Shah, Ullas V Chembazhi, Shivjee Sah, Umesh Varshney

Abstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

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17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

  1. Article
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  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Hijacking Translation Initiation for Synthetic Biology.Chembiochem : a European journal of chemical biology · 2020
    Review
  11. Article
  12. Review
  13. Article
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  17. Review
4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Sunil ShettyDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
Riyaz A ShahDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
Ullas V ChembazhiDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
Shivjee SahDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
Umesh Varshney

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eubacterial translation initiation involves assembly of tRNAfMet, mRNA, initiation factors (IFs) and 30S ribosome in a 30S pre-initiation complex (30S pre-IC), which rearranges and joins 50S ribosome to form 70S IC. Upon releasing IFs, 70S IC becomes elongation-competent 70S. The direct recruitment of initiator tRNA (tRNAfMet) into the ribosomal P-site, crucial in accurate initiation of translation, is attributed to two conserved features of tRNAfMet: (i) formylation of amino acid attached to it and, (ii) the presence of three consecutive G-C base pairs (3GC base pairs) in the anticodon stem. However, the precise roles of these two conserved features of tRNAfMet during the various steps of initiation remain unclear. Using natural and engineered tRNAs, we show that the 3GC pairs license tRNAfMet transitions from 30S to 70S IC and then to elongation-competent 70S by release of IF3. Of the 3GC pairs, the middle GC pair (G30-C40), or merely G30 (in a specific context) suffices in this role and is essential for the sustenance of Escherichia coli. Furthermore, rescue of formylase deficient E. coli by overproduced tRNAfMet reveals that the feature of formylation licenses initial targeting of tRNAfMet to 30S ribosome

Indexed as

Peptide Chain Initiation, TranslationalAnticodonBase PairingEscherichia coliMutationProkaryotic Initiation Factor-3RibosomesRibosome Subunits, Small, BacterialRNA, Transfer, MetAnticodonfMet-tRNA(fMet)Prokaryotic Initiation Factor-3RNA, Transfer, Met

Identifiers

PMID28204695
PMCPMC5389676

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.