<span style="font-size:11.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-bidi-font-family: Mangal;mso-ansi-language:EN-GB;mso-fareast-language:EN-US;mso-bidi-language: HI" lang="EN-GB">Cloning and characterization of 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) gene from <i style="mso-bidi-font-style:normal">Paris</i><i style="mso-bidi-font-style:normal"> fargesii </i>Franch</span>

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 <i style="mso-bidi-font-style: normal">Paris fargesii</i> Franch<i style="mso-bidi-font-style: normal">. </i>The full-length cDNA of <i style="mso-bidi-font-style:normal">P.</i><i style="mso-bidi-font-style:normal"> fargesii HMGR</i> (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<i style="mso-bidi-font-style:normal"> Ricinus communis </i>(77%), <i style="mso-bidi-font-style:normal">Litchi chinensis </i>(76%), <i style="mso-bidi-font-style:normal">Michelia chapensis</i> (75%) and <i style="mso-bidi-font-style:normal">Panax quinquefolius </i>(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.