full2010.pdf - page 102

64
Abstract
The copper chaperone (CCH) gene from latex of
Hevea brasiliensis
was cloned and characterized. The
Hevea brasiliensis
copper chaperone (
HbCCH
) cDNA is 567 bp in length, including a 92 bp 5
c
noncoding region,
a 258 bp open reading frame and 217 bp 3
c
noncoding region. The coding region of
HbCCH
represents a putative
86 amino acid residues with a molecular mass of 9.2 kDa. The deduced amino acid sequence of the
HbCCH
gene
product is highly identical to those of other plant
CCHs
. Three-dimensional structure of HbCCH contains 4
E
-
sheets and 2
D
-helixs. Two conserve regions; the N-terminal metal-biding domain (MXCXXC) and lysine rich at
C-terminal were also observed. The N-terminal metal-biding domain was located between
E
-sheet
1
and
D
-helix
1 while the lysine rich region was found between
D
-helix 2
and
E
-sheet
4. The expression of
HbCCH
gene in
leaves, petioles and stems was higher than that detected in roots of
Hevea
seedlings.
Keywords:
Copper chaperone (CCH),
Hevea brasiliensis
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