Molecular cloning of a novel pathogen-inducible cDNA encoding a putative acyl-CoA synthetase from Capsicum annuum L

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Title
Molecular cloning of a novel pathogen-inducible cDNA encoding a putative acyl-CoA synthetase from Capsicum annuum L
Author(s)
Sang Jik Lee; Mi Chung Suh; Shin Je Kim; Jin Kyung Kwon; Min Woo Kim; Kyung Hee Paek; Do Il Choi; Byung Dong Kim
Bibliographic Citation
Plant Molecular Biology, vol. 46, no. 6, pp. 661-671
Publication Year
2001
Abstract
By means of differential display, a pool of salicylic acid (SA)-induced mRNAs were identified and subsequently their cDNAs were isolated from a cDNA library prepared from SA-induced leaf tissues of hot pepper. One of these cDNA clones, designated CaSIG4, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of CaSIG4 showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. CaSIG4 transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with Xanthomonas campestris pv. vesicatoria race 1. To investigate the cis-acting elements mediating CaSIG4 expression, the CaSIG4 5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential cis-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. Taken together, CaSIG4 encoding a putative acyl-CoA synthetase could function as a plasma membrane-bound protein with a role in signaling in plant defense.
Keyword
Acyl-CoA synthetaseAMP-binding proteinCapsicum annuum LmRNA differential displaySalicylic acidSubcellular localization
ISSN
0167-4412
Publisher
Springer
DOI
http://dx.doi.org/10.1023/A:1011677028605
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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