An Escherichia coli gene in search of a function.
The rrnB gene of Escherichia coli is preceded by an open reading frame, which is cotranscribed with rrnB both in vivo and in vitro. It has earlier been shown that a 289 amino acid protein corresponding to this gene is actually synthesized in E. coli. In this paper we show that: (1.) The transcription of this gene diminishes the stringent response of the P1 promoter of the linked rrnB gene, but this is a cis effect and is not mediated by the protein product of the gene. (2.) The functional integrity of this gene seems to be essential, because efforts to replace it by a plasmid-coded copy mutagenized by Tn5 completely failed. (3.) The protein product of this gene was strongly overproduced by a recombinant plasmid, exploiting the principle of "translational coupling". This overproduction did not change the phenotype of the host cell significantly. The protein was purified to apparent electrophoretic homogeneity.
Balikó
G
G
Institute of Biochemistry, Biological Research Center, Szeged, Hungary.
Raukas
A
A
Boros
I
I
Venetianer
P
P
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics*; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D010957:Plasmids; D012335:RNA, Ribosomal / Q000096:biosynthesis; D012097:Repressor Proteins / Q000235:genetics; D014158:Transcription, Genetic
D001426:Bacterial Proteins; D012335:RNA, Ribosomal; D012097:Repressor Proteins