In:
Journal of Plant Biochemistry and Biotechnology, Springer Science and Business Media LLC, Vol. 30, No. 1 ( 2021-03), p. 92-98
Abstract:
Ferulate-5-hydroxylase (F5H) is a key rate-limiting enzyme for the conversion of guaiacyl monolignol (G-monolignol) to syringyl monolignol (S-monolignol) in the specific synthetic lignin pathway, through the catalysis of the 5-hydroxylation of S-monolignol precursors ferulic acid, conifer aldehyde, and coniferyl alcohol. In this study, we cloned the F5H gene of Populus tomenta ( PtoF5H ), whose product has a highly conserved domain of P450-dependent monooxygenase family. Subcellular localization result demonstrated that PtoF5H protein is an endoplasmic reticulum (ER) resident protein. Furthermore, the PtoF5H was transformed into tobacco in the form of sense- and antisense-, showed that the proportion of S-monolignol increased when PtoF5H gene was overexpressed, suggesting PtoF5H could be used as a target gene for modifying lignin composition. These findings provide further insight into the function of PtoF5H .
Type of Medium:
Online Resource
ISSN:
0971-7811
,
0974-1275
DOI:
10.1007/s13562-020-00574-9
Language:
English
Publisher:
Springer Science and Business Media LLC
Publication Date:
2021
detail.hit.zdb_id:
2206337-7
SSG:
12
