Nucleic Acids Research, 1986, Vol. 14, No. 11 4577-4589
© 1986
Articles |
Structure and gene expression of the E. coli Mn-superoxide dismutase gene
Chemistry Department, University of Maryland Baltimore County, Catonsville, MD 21228, USA
Received October 28, 1985. Revised April 14, 1986. Accepted April 14, 1986.
Superoxide disautase is an enzyne which converts superoxide O2 to hydrogen peroxide. Using a single synthetic oligonucleotide 33mer, we screened the E. coli DNA library and isolated a clone containing the E. coli manganese-superoxide dismutase gene. We detemined the DNA sequence. The analysis of the DNA sequence and in vivo as well as in vitro transcription has shown the following. (1) The DMA sequence suggests two possible promoters. However, only one of then seems active during normal aerobic growth. Purified RNA polynerase initiates in vitro transcription froa the same promoter. It is not clear whether the second promoter is functional. It is possible that this promoter could be activated under different growth conditions. (2) There is an inverted repeat sequence which could form a stem-loop structure downstream of the translation stop codon TAA of the Mn-SOD gene. The results of the analysis of in vivo and in vitro RNA have shown that this is the transcription termination signal. Thus, the Mn-SOD gene constitutes a single gene operon. (3) There is an almost perfect 19 base palindrome at the –35 region. The position and the size of the palindrome suggest that this could be a regulatory site.
*Present address: Frederick Cancer Research Facility, Building 469, Room 141, PO Box B. Frederick, MD 21701, USA
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