Abstract
The bacteriophage lambda cIII gene product regulates the lysogenic pathway by stabilizing the lambda cII regulatory protein. Our results show that the expression of the lambda cIII gene is subject to specific requirements. Tests of a set of cIII-lacZ gene and operon fusions reveal that a sequence upstream of the cIII ribosome binding site is needed for cIII translation. The sequence contains an inefficient RNase III processing site. Furthermore, expression of cIII is drastically reduced in cells lacking RNase III. We have isolated a phage carrying a mutation (r1), which lies in the upstream sequence, that leads to a reduction in cIII translation and inactivates the RNase III processing site. The r1 mutant is nevertheless still dependent on RNase III for cIII translation; r1 reduces cIII translation by a factor of 3 in wild-type cells and by a factor of approximately equal to 30 in an RNase III mutant host. We propose that RNase III stimulates cIII translation by binding to the upstream sequence and thereby exposing the cIII ribosome binding site. This stimulation does not involve RNA cleavage. Consistent with this hypothesis is our finding that, in vitro, unprocessed cIII mRNA is translated, whereas RNase III-cleaved cIII mRNA is not.
MeSH Terms
Bacteriophage lambda/genetics
Binding Sites
Cloning, Molecular
Endoribonucleases/physiology
Gene Expression Regulation
Nucleic Acid Conformation
Protein Biosynthesis
RNA Processing, Post-Transcriptional
RNA, Messenger/genetics
RNA, Viral/genetics
Ribonuclease III
Ribosomes/metabolism
Viral Proteins/genetics
Chemicals
RNA, Messenger
RNA, Viral
Viral Proteins
Endoribonucleases
Ribonuclease III
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Altuvia S
Locker-Giladi H
Koby S
Ben-Nun O
Oppenheim A B
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