Identification and characterization of a set of monocot BAHD monolignol transferases. Issue 1 (3rd February 2022)
- Record Type:
- Journal Article
- Title:
- Identification and characterization of a set of monocot BAHD monolignol transferases. Issue 1 (3rd February 2022)
- Main Title:
- Identification and characterization of a set of monocot BAHD monolignol transferases
- Authors:
- Smith, Rebecca A
Beebe, Emily T
Bingman, Craig A
Vander Meulen, Kirk
Eugene, Alexis
Steiner, Alexander J
Karlen, Steven D
Ralph, John
Fox, Brian G - Abstract:
- Abstract: Plant BAHD acyltransferases perform a wide range of enzymatic tasks in primary and secondary metabolism. Acyl-CoA monolignol transferases, which couple a CoA substrate to a monolignol creating an ester linkage, represent a more recent class of such acyltransferases. The resulting conjugates may be used for plant defense but are also deployed as important "monomers" for lignification, in which they are incorporated into the growing lignin polymer chain. p -Coumaroyl-CoA monolignol transferases (PMTs) increase the production of monolignol p -coumarates, and feruloyl-CoA monolignol transferases (FMTs) catalyze the production of monolignol ferulate conjugates. We identified putative FMT and PMT enzymes in sorghum ( Sorghum bicolor ) and switchgrass ( Panicum virgatum ) and have compared their activities to those of known monolignol transferases. The putative FMT enzymes produced both monolignol ferulate and monolignol p -coumarate conjugates, whereas the putative PMT enzymes produced monolignol p -coumarate conjugates. Enzyme activity measurements revealed that the putative FMT enzymes are not as efficient as the rice ( Oryza sativa ) control OsFMT enzyme under the conditions tested, but the SbPMT enzyme is as active as the control OsPMT enzyme. These putative FMTs and PMTs were transformed into Arabidopsis ( Arabidopsis thaliana ) to test their activities and abilities to biosynthesize monolignol conjugates for lignification in planta. The presence of ferulates and pAbstract: Plant BAHD acyltransferases perform a wide range of enzymatic tasks in primary and secondary metabolism. Acyl-CoA monolignol transferases, which couple a CoA substrate to a monolignol creating an ester linkage, represent a more recent class of such acyltransferases. The resulting conjugates may be used for plant defense but are also deployed as important "monomers" for lignification, in which they are incorporated into the growing lignin polymer chain. p -Coumaroyl-CoA monolignol transferases (PMTs) increase the production of monolignol p -coumarates, and feruloyl-CoA monolignol transferases (FMTs) catalyze the production of monolignol ferulate conjugates. We identified putative FMT and PMT enzymes in sorghum ( Sorghum bicolor ) and switchgrass ( Panicum virgatum ) and have compared their activities to those of known monolignol transferases. The putative FMT enzymes produced both monolignol ferulate and monolignol p -coumarate conjugates, whereas the putative PMT enzymes produced monolignol p -coumarate conjugates. Enzyme activity measurements revealed that the putative FMT enzymes are not as efficient as the rice ( Oryza sativa ) control OsFMT enzyme under the conditions tested, but the SbPMT enzyme is as active as the control OsPMT enzyme. These putative FMTs and PMTs were transformed into Arabidopsis ( Arabidopsis thaliana ) to test their activities and abilities to biosynthesize monolignol conjugates for lignification in planta. The presence of ferulates and p -coumarates on the lignin of these transformants indicated that the putative FMTs and PMTs act as functional feruloyl-CoA and p -coumaroyl-CoA monolignol transferases within plants. Abstract : A group of identified BAHD acyltransferases function as feruloyl-CoA monolignol transferases and/or p -coumaroyl-CoA monolignol transferases in vitro and in planta. … (more)
- Is Part Of:
- Plant physiology. Volume 189:Issue 1(2022)
- Journal:
- Plant physiology
- Issue:
- Volume 189:Issue 1(2022)
- Issue Display:
- Volume 189, Issue 1 (2022)
- Year:
- 2022
- Volume:
- 189
- Issue:
- 1
- Issue Sort Value:
- 2022-0189-0001-0000
- Page Start:
- 37
- Page End:
- 48
- Publication Date:
- 2022-02-03
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1093/plphys/kiac035 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 26751.xml