Abstract:
:This work describes the isolation of mutations in infC, the structural gene for IF3, using different genetic screens. Among 21 mutants characterised, seven were shown to produce stable variant IF3 proteins unable to fully complement a strain carrying a chromosomal deletion of the infC gene. The mutants were also shown to be unable to normally discriminate against several non-canonical initiation codons such as AUU and ACG. The two mutants with the strongest complementation or discrimination defects carry changes in the C-terminal domain of IF3, which is responsible for the binding of the factor to the 30 S ribosomal subunit. We show that the first mutant has an expected decreased but the second an unexpected increased capacity to bind the 30 S subunit. The in vivo defects of the second mutant are explained by its capacity to bind unspecifically to other targets, as shown by its increased affinity for the 50 S subunit, which is normally not recognised by the factor. Interestingly, this mutant corresponds to a change of an acidic residue that might play a negative discriminatory role in preventing interactions with non-cognate RNAs, as has been reported for acidic residues of aminoacyl-tRNA synthetases shown to be involved in tRNA recognition.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Sacerdot C,de Cock E,Engst K,Graffe M,Dardel F,Springer Mdoi
10.1006/jmbi.1999.2737keywords:
subject
Has Abstractpub_date
1999-05-21 00:00:00pages
803-10issue
5eissn
0022-2836issn
1089-8638pii
S0022-2836(99)92737-7journal_volume
288pub_type
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journal_title:Journal of molecular biology
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journal_title:Journal of molecular biology
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journal_title:Journal of molecular biology
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