A mutation in ribosomal protein L9 affects ribosomal hopping during translation of gene 60 from bacteriophage T4

Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12525-9. doi: 10.1073/pnas.91.26.12525.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage T4 / genetics*
  • Base Sequence
  • DNA Primers / chemistry
  • Escherichia coli / genetics
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Nucleic Acid Conformation
  • Protein Biosynthesis*
  • RNA, Messenger / genetics
  • Ribosomal Proteins / metabolism*
  • Ribosomes / metabolism*
  • Structure-Activity Relationship

Substances

  • DNA Primers
  • RNA, Messenger
  • Ribosomal Proteins
  • ribosomal protein L9