Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/29084
Title: Cloning and characterization of 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) gene from Paris fargesii Franch
Authors: Liang, Yili
Jiang, XueMei
Hu, Qi
Li, Xiaoqi
HuaqunYin
Li, Diqiang
Zhang, Yuguang
Liu, Xueduan
Keywords: Paris fargesii Franch;3-Hydroxy-3-methylglutaryl-CoA reductase (HMGR);Cloning;RACE
Issue Date: Jun-2014
Publisher: NISCAIR-CSIR, India
Abstract: 3-Hydroxy-3-methylglutaryl-coenzyme A reductase (HMGR) plays an important role in catalyzing the first committed step of isoprenoids biosynthesis in mevalonic acid (MVA) pathway. Here, we cloned a full-length transcript of Paris fargesii Franch. The full-length cDNA of P. fargesii HMGR (Pf-HMGR, GenBank accession no. JX508638) was 1,973 bp and contained a 1,728 bp ORF encoding 576 amino acids. Sequence analysis revealed that the deduced Pf-HMGR had high similarity with HMGRs from other plants, including Ricinus communis (77%), Litchi chinensis (76%), Michelia chapensis (75%) and Panax quinquefolius (72%). It had a calculated molecular mass of about 62.13 kDa and an isoelectric point (pI) of 8.47. It contained two transmembrane domains, two putative HMGR binding sites and two NADP(H)-binding sites. The predicted 3-D structure revealed that Pf-HMGR had a similar spatial structure with other plant HMGRs. Three catalytic regions, including L-domain, N-domain and S-domain were detected by structural modeling of HMGR. Tissue expression analysis revealed that Pf-HMGR was strongly expressed in roots and stems than in leaves. Taken together, our data laid a foundation for further investigation of HMGR's functions and regulatory mechanisms in plants.
Page(s): 201-206
URI: http://hdl.handle.net/123456789/29084
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.51(3) [June 2014]

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