Abstract
Oligoribonuclease, a 3'-to-5' exoribonuclease specific for small oligoribonucleotides, was purified to homogeneity from extracts of Escherichia coli. The purified protein is an α2 dimer of 40 kDa. NH2- terminal sequence analysis of the protein identified the gene encoding oligoribonuclease as yjeR (o204a), a previously reported open reading frame located at 94 min on the E. coli chromosome. However, as a consequence of the sequence information, the translation start site of this open reading frame has been revised. Cloning of yjeR led to overexpression of oligoribonuclease activity, and interruption of the cloned gene with a kanamycin resistance cassette eliminated the overexpression. On the basis of these data, we propose that yjeR be renamed orn. Orthologs of oligoribonuclease are present in a wide range of organisms, extending up to humans.
| Original language | English |
|---|---|
| Pages (from-to) | 2779-2781 |
| Number of pages | 3 |
| Journal | Journal of Bacteriology |
| Volume | 180 |
| Issue number | 10 |
| State | Published - May 1 1998 |
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ASJC Scopus subject areas
- Applied Microbiology and Biotechnology
- Immunology
Cite this
Oligoribonuclease is encoded by a highly conserved gene in the 3'-5' exonuclease superfamily. / Zhang, Xiaolan; Zhu, Liuqin; Deutscher, Murray P.
In: Journal of Bacteriology, Vol. 180, No. 10, 01.05.1998, p. 2779-2781.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Oligoribonuclease is encoded by a highly conserved gene in the 3'-5' exonuclease superfamily
AU - Zhang, Xiaolan
AU - Zhu, Liuqin
AU - Deutscher, Murray P
PY - 1998/5/1
Y1 - 1998/5/1
N2 - Oligoribonuclease, a 3'-to-5' exoribonuclease specific for small oligoribonucleotides, was purified to homogeneity from extracts of Escherichia coli. The purified protein is an α2 dimer of 40 kDa. NH2- terminal sequence analysis of the protein identified the gene encoding oligoribonuclease as yjeR (o204a), a previously reported open reading frame located at 94 min on the E. coli chromosome. However, as a consequence of the sequence information, the translation start site of this open reading frame has been revised. Cloning of yjeR led to overexpression of oligoribonuclease activity, and interruption of the cloned gene with a kanamycin resistance cassette eliminated the overexpression. On the basis of these data, we propose that yjeR be renamed orn. Orthologs of oligoribonuclease are present in a wide range of organisms, extending up to humans.
AB - Oligoribonuclease, a 3'-to-5' exoribonuclease specific for small oligoribonucleotides, was purified to homogeneity from extracts of Escherichia coli. The purified protein is an α2 dimer of 40 kDa. NH2- terminal sequence analysis of the protein identified the gene encoding oligoribonuclease as yjeR (o204a), a previously reported open reading frame located at 94 min on the E. coli chromosome. However, as a consequence of the sequence information, the translation start site of this open reading frame has been revised. Cloning of yjeR led to overexpression of oligoribonuclease activity, and interruption of the cloned gene with a kanamycin resistance cassette eliminated the overexpression. On the basis of these data, we propose that yjeR be renamed orn. Orthologs of oligoribonuclease are present in a wide range of organisms, extending up to humans.
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M3 - Article
C2 - 9573169
AN - SCOPUS:0031924593
VL - 180
SP - 2779
EP - 2781
JO - Journal of Bacteriology
JF - Journal of Bacteriology
SN - 0021-9193
IS - 10
ER -