Worm Breeder's Gazette 12(2): 42 (January 1, 1992)

These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.

Cloning of manganese superoxide dismutase in C. elegans

Norio Suzuki, Naoaki Ishii, Kenshi Suzuki

Figure 1

Department of Molecular Biology, Tokai University School of Medicine, Isehara, Kanagawa Japan 259-11

The reduction of molecular oxygen in all aerobic cells results in intermediates (superoxide radicals, hydrogen peroxide and hydroxy ions) which are highly toxic. Superoxide radicals may play an important role in aging. Superoxide dismutase (SOD) are metalloenzyme which eliminate, through a dismutation reaction, superoxide radicals produced within cells. There are two distinct types of SOD in eukaryotic cells. The copper- and zinc-containing enzyme (CuZn SOD) is found principally in the cytosole and the manganese-containing enzyme (Mn SOD) is found exclusively in the mitochondorial matrix. Pamela Larsen has cloned the Cu-Zn SOD in C. elegans and sequenced (Gazetti, Vol. 11 No. 5, p. 27).

Now we cloned and sequenced the Mn SOD in C. elegans. One oligonucleotide was designed from the highly conserved regions that be found in Mn SOD gene which has cloned from several animals. The oligonucleotide was used as probe to hybridize with Barstead cDNA library.

[See Figure 1]

Figure 1