Multiple defects in translation associated with altered ribosomal protein L4.

Abstract:

:The ribosomal proteins L4 and L22 form part of the peptide exit tunnel in the large ribosomal subunit. In Escherichia coli, alterations in either of these proteins can confer resistance to the macrolide antibiotic, erythromycin. The structures of the 30S as well as the 50S subunits from each antibiotic resistant mutant differ from wild type in distinct ways and L4 mutant ribosomes have decreased peptide bond-forming activity. Our analyses of the decoding properties of both mutants show that ribosomes carrying the altered L4 protein support increased levels of frameshifting, missense decoding and readthrough of stop codons during the elongation phase of protein synthesis and stimulate utilization of non-AUG codons and mutant initiator tRNAs at initiation. L4 mutant ribosomes are also altered in their interactions with a range of 30S-targeted antibiotics. In contrast, the L22 mutant is relatively unaffected in both decoding activities and antibiotic interactions. These results suggest that mutations in the large subunit protein L4 not only alter the structure of the 50S subunit, but upon subunit association, also affect the structure and function of the 30S subunit.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

O'Connor M,Gregory ST,Dahlberg AE

doi

10.1093/nar/gkh913

keywords:

subject

Has Abstract

pub_date

2004-10-27 00:00:00

pages

5750-6

issue

19

eissn

0305-1048

issn

1362-4962

pii

32/19/5750

journal_volume

32

pub_type

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