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Isolation and Characterization of a Histidine Biosynthetic Gene
in Arabidopsis Encoding a Polypeptide with Two Separate Domains for
Phosphoribosyl-ATP Pyrophosphohydrolase and Phosphoribosyl-AMP
Cyclohydrolase
Ko Fujimori and
Daisaku Ohta*
Takarazuka Research Institute, Novartis Pharma K.K., 10-66 Miyuki-cho, Takarazuka 665-8666, Japan (K.F.); and Research Institute
for Biological Sciences, Okayama, 7549-1 Yoshikawa, Kayo-cho,
Okayama 716-1241, Japan (D.O.)
Phosphoribosyl-ATP
pyrophosphohydrolase (PRA-PH) and phosphoribosyl-AMP cyclohydrolase
(PRA-CH) are encoded by HIS4 in yeast and by
hisIE in bacteria and catalyze the second and the third step, respectively, in the histidine biosynthetic pathway. By complementing a hisI mutation of Escherichia
coli with an Arabidopsis cDNA library, we isolated an
Arabidopsis cDNA (At-IE) that possesses these two enzyme activities.
The At-IE cDNA encodes a bifunctional protein of 281 amino acids with a
calculated molecular mass of 31,666 D. Genomic DNA-blot analysis with
the At-IE cDNA as a probe revealed a single-copy gene in Arabidopsis,
and RNA-blot analysis showed that the At-IE gene was
expressed ubiquitously throughout development. Sequence comparison
suggested that the At-IE protein has an N-terminal extension of about
50 amino acids with the properties of a chloroplast transit peptide. We
demonstrated through heterologous expression studies in E. coli that the functional domains for the PRA-CH (hisI) and
PRA-PH (hisE) resided in the N-terminal and the C-terminal halves,
respectively, of the At-IE protein.
*
Corresponding author; e-mail ohtad{at}orange.ocn.ne.jp; fax
81-866-56-9454.
Plant Physiol. (1998) 118: 275-283
Copyright Clearance Center: 0032-0889/98/118//09
© 1998 American Society of Plant Physiologists
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