Two cDNAs encode two nearly identical Cu/Zn superoxide dismutase proteins in maize.

Molecular & General Genetics : MGG
R E Cannon, J G Scandalios

Abstract

SOD-4, a cytosolic form of superoxide dismutase in maize, originally was defined as a single band of activity by zymogram analysis. The protein was purified to "homogeneity" as shown by a single band on native or denaturing polyacrylamide gels and a single spot on two dimensional gels. The N-terminal amino acid sequence for the first 20 residues was determined for the purified SOD-4 protein. All residues were clearly determined except for residue twelve, where both glutamic and aspartic acids were found. A maize lambda gt11 cDNA library was constructed from scutellar poly(A)+ RNA. Two cDNAs were isolated, restriction mapped, and their DNA sequences determined. The amino acid sequence deduced from both cDNAs matched perfectly the N-terminal sequence of the purified protein except for the residue at position 12. Significantly, at the twelfth codon, one cDNA was found to code for glutamic acid and the other cDNA had a codon for aspartic acid. Both cDNAs contained similar but not identical 5' and 3' untranslated sequences. Both cDNAs contained polyadenylation signals and tails. cDNA isolations, RNA, and genomic DNA blots confirm the existence and expression of two genes that produce indistinguishable SOD-4 proteins.

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Citations

Feb 1, 1992·Plant Molecular Biology·S KarpinskiJ E Hällgren
Nov 1, 1992·Free Radical Biology & Medicine·L A del RíoF J Corpas
Jan 1, 1997·Free Radical Biology & Medicine·W Van CampM Van Montagu
Mar 15, 2005·Plant Physiology and Biochemistry : PPB·Seung-Yong ShinSang-Soo Kwak
Nov 1, 1990·TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·A Acevedo, J G Scandalios
May 1, 1992·The Plant Journal : for Cell and Molecular Biology·J D Williamson, J G Scandalios

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