Journal of Experimental Botany, Vol 49, 1625-1636, Copyright © 1998 by Oxford University Press
A Warrilow and M Hawkesford
Cysteine synthase (O-acetylserine (thiol) lyase, EC
4.2.99.8) and
ARTICLES
Separation, subcellular location and influence of sulphur nutrition on isoforms of cysteine synthase in spinach
IACR-Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS41 9AF, UK; Corresponding author at: IACR-Rothamsted, Biochemistry and Physiology Department, Harpenden, Hertfordshire AL5 2JQ, UK
-cyanoalanine synthase (EC
4.4.1.9) have been isolated from leaves of Spinacea
oleracea L. and separated by anion-exchange chromatography.
Further separation of one minor and two major isoforms of cysteine synthase
was achieved by hydrophobic interaction chromatography and high resolution
native electrophoresis (PAGE). Analysis of root material indicated that
amongst the multiple isoforms present, a single isoform predominated.
Subcellular fractionation studies indicated that one of the major leaf
forms, cysteine synthase B, was located in the chloroplast and the other,
cysteine synthase B, occurred in the cytoplasm. No specific isoform of
cysteine synthase was resolved in the mitochondria, while cyanoalanine
synthase was predominantly located in the mitochondrial fraction. Sulphur
deprivation decreased cysteine synthase activity, but not cyanalanine
synthase activity in both young and mature leaves, although cysteine
synthase activity in the roots increased slightly. A selective decrease in
cystein synthase B (chloroplastic abundance was observed in mature leaves.
Patterns of expression of cysteine synthase in response to S-availability
are discussed in relation to possible roles for this enzyme in controlling
S-flux through the S-assimilatory pathway.Key words: Cysteine synthase
isoforms (expression of), Spinacea oleracea L.,
sulphur deficiency.
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