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A Gene Encoding the Cytokinin Enzyme Zeatin
O-Xylosyltransferase of Phaseolus
vulgaris1
Ruth C. Martin,
Machteld C. Mok, and
David W.S. Mok*
Department of Horticulture and Center for Gene Research and
Biotechnology, Oregon State University, Corvallis, Oregon
97331-7304
Zeatin is the most active and
ubiquitous form of the naturally occurring cytokinins. Glycosyl
conjugates of zeatin are found in many plant tissues and are considered
important for storage and protection against degradative enzymes. Two
enzymes catalyzing the formation of O-glycosyl
derivatives of zeatin have been characterized, O-glucosyltransferase and
O-xylosyltransferase, occurring in seeds of lima bean
(Phaseolus lunatus) and bean (Phaseolus
vulgaris), respectively. Recently, the ZOG1 gene
(zeatin
O-glucosyltansferase) was
isolated from P. lunatis (). Based on
the ZOG1 sequence, the ZOX1 gene
(zeatin
O-xylosyltransferase) was cloned from P. vulgaris. ZOX1
contains an open reading frame of 1362 bp that codes for a 454-amino
acid peptide of 51 kD. The recombinant protein has properties identical
to the native enzyme: it catalyzes O-xylosylzeatin
formation with UDP-Xyl as a glycosyl donor but does not recognize
UDP-Glucose as a substrate. The ZOX1 and
ZOG1 genes exhibit 93% identity at the nucleotide level
and 90% similarity at the amino acid level. Neither gene contains introns. These zeatin-specific genes and their promoters will be useful
for studies of the regulation of active versus storage forms of
cytokinins. Comparison of sequences encoding similar enzymes with
distinct substrate specificity may lead to identification of epitopes
specific to cytokinin and glycosyl donor molecules.
1
This research was supported by a grant from the
U.S. Department of Agriculture-National Research Initiative Competitive
Grants Program (no. 9801398) and the Oregon Agricultural Experiment
Station (paper no. 11,466).
*
Corresponding author; e-mail mokd{at}bcc.orst.edu; fax
1-541-737-3479.
Plant Physiol. (1999) 120: 553-558
Copyright Clearance Center: 0032-0889/99/120//06
© 1999 American Society of Plant Physiologists
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