Evidence map›Paper›PMID 35477794›Full record

ArticlePlant physiology2022

Natural variation meets synthetic biology: Promiscuous trichome-expressed acyltransferases from Nicotiana.

Craig A Schenck, Thilani M Anthony, MacKenzie Jacobs, A Daniel Jones, Robert L Last

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 15 citations in OpenAlex.

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  6. Trading acyls and swapping sugars: metabolic innovations inbioRxiv : the preprint server for biology · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Craig A SchenckDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, USA.ORCID 0000-0002-5711-7213
Thilani M AnthonyDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, USA.ORCID 0000-0003-3270-6182
MacKenzie JacobsDepartment of Physical Sciences and Mathematics, West Liberty University, West Liberty, West Virginia 26074, USA.ORCID 0000-0003-0113-1224
A Daniel JonesDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, USA.ORCID 0000-0002-7408-6690
Robert L LastDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, USA.ORCID 0000-0001-6974-9587
Michigan State University · USWest Liberty University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acylsugars are defensive, trichome-synthesized sugar esters produced in plants across the Solanaceae (nightshade) family. Although assembled from simple metabolites and synthesized by a relatively short core biosynthetic pathway, tremendous within- and across-species acylsugar structural variation is documented across the family. To advance our understanding of the diversity and the synthesis of acylsugars within the Nicotiana genus, trichome extracts were profiled across the genus coupled with transcriptomics-guided enzyme discovery and in vivo and in vitro analysis. Differences in the types of sugar cores, numbers of acylations, and acyl chain structures contributed to over 300 unique annotated acylsugars throughout Nicotiana. Placement of acyl chain length into a phylogenetic context revealed that an unsaturated acyl chain type was detected in a few closely related species. A comparative transcriptomics approach identified trichome-enriched Nicotiana acuminata acylsugar biosynthetic candidate enzymes. More than 25 acylsugar variants could be produced in a single enzyme assay with four N. acuminata acylsugar acyltransferases (NacASAT1-4) together with structurally diverse acyl-CoAs and sucrose. Liquid chromatography coupled with mass spectrometry screening of in vitro products revealed the ability of these enzymes to make acylsugars not present in Nicotiana plant extracts. In vitro acylsugar production also provided insights into acyltransferase acyl donor promiscuity and acyl acceptor specificity as well as regiospecificity of some ASATs. This study suggests that promiscuous Nicotiana acyltransferases can be used as synthetic biology tools to produce novel and potentially useful metabolites.

Indexed as

AcyltransferasesTrichomesCarbohydratesNicotianaPhylogenyPlant ProteinsSugarsSynthetic BiologyAcyltransferasesCarbohydratesPlant ProteinsSugars

Identifiers

PMID35477794
PMCPMC9434288
OpenAlexW4225089712

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.