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4. Cysteine biosynthesis in higher plants: a new member of the Arabidopsis thaliana serine acetyltransferase small gene-family obtained by functional complementation of an Escherichia coli cysteine auxotroph.

Author

Howarth JR, Roberts MA, and Wray JL

Subjects
Acetyltransferases chemistry, Amino Acid Sequence, Arabidopsis enzymology, Base Sequence, Cloning, Molecular, DNA, Complementary genetics, DNA, Plant genetics, Escherichia coli genetics, Escherichia coli metabolism, Genetic Complementation Test, Molecular Sequence Data, Molecular Weight, Mutation, Open Reading Frames, Sequence Homology, Amino Acid, Serine O-Acetyltransferase, Acetyltransferases genetics, Arabidopsis genetics, Arabidopsis metabolism, Cysteine biosynthesis, Genes, Plant, Multigene Family
Abstract

A cDNA clone, Sat-52, encoding a novel isoform of serine acetyltransferase (EC 2.3.1.30) was isolated by functional complementation of an Escherichia coli cysE mutant defective in serine acetyltransferase. The 1158 base pair clone contains a full-length open reading frame encoding a deduced protein of 312 amino acids with an M(r) of 32.77 kDa. Northern analysis revealed a single transcript of ca 1.19 kb that did not increase in abundance under sulfate limitation. Genomic Southern hybridization suggests the presence of a single copy of the Sat-52 gene.

Published
1997
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