A mutation in ribosomal protein L9 affects ribosomal hopping during translation of gene 60 from bacteriophage T4.
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.
Herbst
K L
KL
Howard Hughes Medical Institute, University of Utah, Salt Lake City 84112.
Nichols
L M
LM
Gesteland
R F
RF
Weiss
R B
RB
D000595:Amino Acid Sequence; D017122:Bacteriophage T4 / Q000235:genetics*; D001483:Base Sequence; D017931:DNA Primers / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D013329:Structure-Activity Relationship
D017931:DNA Primers; D012333:RNA, Messenger; D012269:Ribosomal Proteins; C049650:ribosomal protein L9