Weakening the IF2-fMet-tRNA Interaction Suppresses the Lethal Phenotype Caused by GTPase Inactivation.

doi:10.3390/ijms222413238

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Weakening the IF2-fMet-tRNA Interaction Suppresses the Lethal Phenotype Caused by GTPase Inactivation.

International journal of molecular sciences - 8 Dec 2021

Tomsic Jerneja, Caserta Enrico, Pon Cynthia L, Gualerzi Claudio O

Abstract excerpt

Substitution of the conserved Histidine 448 present in one of the three consensus elements characterizing the guanosine nucleotide binding domain (IF2 G2) of Escherichia coli translation initiation factor IF2 resulted in impaired ribosome-dependent GTPase activity which prevented IF2 dissociation from the ribosome, caused a severe protein synthesis inhibition, and yielded a dominant lethal phenotype. A reduced...

Topics

Escherichia coli
Escherichia coli Proteins
GTP Phosphohydrolases
Genes, Lethal
Guanosine Triphosphate
Hydrolysis
Models, Molecular
Phenotype
Prokaryotic Initiation Factor-2
Protein Conformation
Protein Domains
RNA, Transfer, Met
Ribosomes

Source

Open in PubMed Open full text

Identifiers

PMID: 34948034
DOI: 10.3390/ijms222413238
PMCID: PMC8709274

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics