کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5747699 1618924 2017 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The phytochelatin synthase gene in date palm (Phoenix dactylifera L.): Phylogeny, evolution and expression
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم محیط زیست شیمی زیست محیطی
پیش نمایش صفحه اول مقاله
The phytochelatin synthase gene in date palm (Phoenix dactylifera L.): Phylogeny, evolution and expression
چکیده انگلیسی


- A 5764 base pair sequence encoding PdPCS1 (Pdpcs) was found.
- pcs gene history has been studied.
- Pdpcs1 gene expression was measured in seedling hypocotyls exposed to Cd, Cu and Cr.
- Phytochelatin synthase type I enzyme was identified in date palm (PdPCS1).

We studied date palm phytochelatin synthase type I (PdPCS1), which catalyzes the cytosolic synthesis of phytochelatins (PCs), a heavy metal binding protein, in plant cells. The gene encoding PdPCS1 (Pdpcs) consists of 8 exons and 7 introns and encodes a protein of 528 amino acids. PCs gene history was studied using Notung phylogeny. During evolution, gene loss from several lineages was predicted including Proteobacteria, Bilateria and Brassicaceae. In addition, eleven gene duplication events appeared toward interior nodes of the reconciled tree and four gene duplication events appeared toward the external nodes. These latter sequences belong to species with a second copy of PCs suggesting that this gene evolved through subfunctionalization. Pdpcs1 gene expression was measured in seedling hypocotyls exposed to Cd, Cu and Cr using quantitative real-time polymerase chain reaction (qPCR). A Pdpcs1 overexpression was evidenced in P. dactylifera seedlings exposed to metals suggesting that 1-the Pdpcs1 gene is functional, 2-there is an implication of the enzyme in metal detoxification mechanisms. Additionally, the structure of PdPCS1 was predicted using its homologue from Nostoc (cyanobacterium, NsPCS) as a template in Discovery studio and PyMol software. These analyses allowed us to identify the phytochelatin synthase type I enzyme in date palm (PdPCS1) via recognition of key consensus amino acids involved in the catalytic mechanism, and to propose a hypothetical binding and catalytic site for an additional substrate binding cavity.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Ecotoxicology and Environmental Safety - Volume 140, June 2017, Pages 7-17
نویسندگان
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