Reference "Characterization and heterospecific expression of cDNA clones of genes in the maize GSH S-transferase multigene family"

Reference ID

7212

Title

Characterization and heterospecific expression of cDNA clones of genes in the maize GSH S-transferase multigene family

Source

Nucleic acids research, 1988, vol. 16, pp. 425-438

Authors (6)

Grove-G	Zarlengo-R-P
Timmerman-K-P	Li-N-Q
Tam-M-F	Tu-C-P

Abstract

We have isolated from a constructed lambda gt11 expression library two classes
of cDNA clones encoding the entire sequence of the maize GSH S-transferases
GST I and GST III. Expression of a full-length GST I cDNA in E. coli resulted
in the synthesis of enzymatically active maize GST I that is immunologically
indistinguishable from the native GST I. Another GST I cDNA with a truncated
N-terminal sequence is also active in heterospecific expression. Our GST III
cDNA sequence differs from the version reported by Moore et al. [Moore, R. E.,
Davies, M. S., O'Connell, K. M., Harding, E. I., Wiegand, R. C., and Tiemeier,
D. C. (1986) Nucleic Acids Res. 14:7227-7235] in eight reading frame shifts
which result in partial amino acid sequence conservation with the rat GSH S-
transferase sequences. The GST I and GST III sequences share approximately 45%
amino acid sequence homology. Both the GST I and the GST III mRNAs contain
different repeating motifs in front of the initiation codon ATG. Multiple
poly(A) addition sites have been identified for these two classes of maize GSH
S-transferase messages. Genomic Southern blotting results suggest that both
GST I and GST III are present in single or low copies in the maize (GT112
RfRf) genome.