Open AccessA mutation in ribosomal protein L9 affects ribosomal hopping during translation of gene 60 from bacteriophage T4.
Author(s) -
Karen L. Herbst,
Lindy M. Nichols,
Raymond F. Gesteland,
Robert B. Weiss
Publication year - 1994
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.91.26.12525
Subject(s) - ribosome , biology , ribosomal protein , ribosomal rna , genetics , gene , coding region , microbiology and biotechnology , 30s , bacteriophage , mutant , rna , escherichia coli
Ribosomes hop over a 50-nt coding gap during translation of gene 60 mRNA from bacteriophage T4. This event occurs with near-unitary efficiency when gene 60-lacZ fusions are expressed in Escherichia coli. One of the components necessary for this hop is an RNA hairpin structure containing the 5' junction of the 50-nt coding gap. A mutant E. coli was isolated and found to significantly increase hopping when carrying gene 60-lacZ constructs with altered hairpins. The mutation, hop-1, changed Ser93 to Phe in rplI, the gene coding for ribosomal large-subunit protein L9. Ribosomal hopping on a synthetic sequence in the absence of a hairpin was also increased by this mutation. These data suggest that hop-1 may substitute for the function of the hairpin during ribosomal hopping.