scholarly journals Characterization of Developmental- and Stress-Mediated Expression of Cinnamoyl-CoA Reductase in Kenaf (Hibiscus cannabinusL.)

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Ritesh Ghosh ◽  
Bosung Choi ◽  
Byoung-Kwan Cho ◽  
Hyoun-Sub Lim ◽  
Sang-Un Park ◽  
...  

Cinnamoyl-CoA reductase (CCR) is an important enzyme for lignin biosynthesis as it catalyzes the first specific committed step in monolignol biosynthesis. We have cloned a full length coding sequence ofCCRfrom kenaf (Hibiscus cannabinusL.), which contains a 1,020-bp open reading frame (ORF), encoding 339 amino acids of 37.37 kDa, with an isoelectric point (pI) of 6.27 (JX524276,HcCCR2). BLAST result found that it has high homology with other plant CCR orthologs. Multiple alignment with other plant CCR sequences showed that it contains two highly conserved motifs: NAD(P) binding domain (VTGAGGFIASWMVKLLLEKGY) at N-terminal and probable catalytic domain (NWYCYGK). According to phylogenetic analysis, it was closely related to CCR sequences ofGossypium hirsutum(ACQ59094) andPopulus trichocarpa(CAC07424).HcCCR2showed ubiquitous expression in various kenaf tissues and the highest expression was detected in mature flower.HcCCR2was expressed differentially in response to various stresses, and the highest expression was observed by drought and NaCl treatments.

2004 ◽  
Vol 31 (1) ◽  
pp. 73 ◽  
Author(s):  
Zhihua Liao ◽  
Qiumin Tan ◽  
Yourong Chai ◽  
Kaijing Zuo ◽  
Min Chen ◽  
...  

In plants, the first committed step in the pathway for biosynthesis of isoprenoids is catalysed by 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR, EC: 1.1.1.34). Here we report for the first time the cloning of a full-length cDNA encoding HMGR (Tm–HMGR) from a taxol-producing gymnosperm, Taxus media Rehder. The full-length cDNA of Tm–HMGR (GenBank accession number: AY277740) was 2307 base pairs (bp), with a 1791-bp open reading frame (ORF) encoding a 596-amino-acid polypeptide. Bioinformatic analysis revealed that Tm–HMGR contained two trans-membrane domains and a catalytic domain, and showed high homology to other plant HMGRs. Phylogenetic analysis indicated that Tm–HMGR was more ancient than other plant HMGRs. The structural modelling showed that Tm–HMGR had the typical spatial structure of HMGRs whose catalytic domains could be folded and divided into three spatial domains, L-domain, N-domain and S-domain. Southern blot analysis revealed that Tm–HMGR belonged to a small HMGR gene family. Northern blot analysis showed that Tm–HMGR was expressed in roots, stems and needles, with higher expression in stems and needles than in roots. Functional complementation of Tm–HMGR in a HMGR-deficient mutant yeast demonstrated that Tm–HMGR mediated the biosynthesis of mevalonate and provided the general precursor for taxol biosynthesis.


PeerJ ◽  
2021 ◽  
Vol 9 ◽  
pp. e10741
Author(s):  
Nan Chao ◽  
Qi Qi ◽  
Shuang Li ◽  
Brent Ruan ◽  
Xiangning Jiang ◽  
...  

Hydroxycinnamoyl-CoA: shikimate hydroxycinnamoyl transferase (HCT) divides the mass flux to H, G and S units in monolignol biosynthesis and affects lignin content. Ten HCT homologs were identified in the Populus trichocarpa (Torr. & Gray) genome. Both genome duplication and tandem duplication resulted in the expansion of HCT orthologs in Populus. Comprehensive analysis including motif analysis, phylogenetic analysis, expression profiles and co-expression analysis revealed the divergence and putative function of these candidate PoptrHCTs. PoptrHCT1 and 2 were identified as likely involved in lignin biosynthesis. PoptrHCT9 and 10- are likely to be involved in plant development and the response to cold stress. Similar functional divergence was also identified in Populus tomentosa Carr. Enzymatic assay of PtoHCT1 showed that PtoHCT1 was able to synthesize caffeoyl shikimate using caffeoyl-CoA and shikimic acid as substrates.


2010 ◽  
Vol 38 (3) ◽  
pp. 2075-2083 ◽  
Author(s):  
Yongsheng Hu ◽  
Peng Di ◽  
Junfeng Chen ◽  
Ying Xiao ◽  
Lei Zhang ◽  
...  

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