Evidence map›Paper›PMID 21193570›Full record

ArticleThe Plant cell2010

LAP6/POLYKETIDE SYNTHASE A and LAP5/POLYKETIDE SYNTHASE B encode hydroxyalkyl α-pyrone synthases required for pollen development and sporopollenin biosynthesis in Arabidopsis thaliana.

Sung Soo Kim, Etienne Grienenberger, Benjamin Lallemand, Che C Colpitts, Sun Young Kim, Clarice de Azevedo Souza, Pierrette Geoffroy, Dimitri Heintz, Daniel Krahn, Markus Kaiser and 5 more

Open access · hybridAbstract readValidation Study
In one paragraph

Article in The Plant cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

107 citing papers in PubMed, 222 citations in OpenAlex.

  1. Review
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47 more citing papers are in PubMed but not listed here.

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

15 authors at 6 institutions in 3 countries.

Sung Soo KimDepartment of Botany, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada.
Etienne Grienenberger
Benjamin Lallemand
Che C Colpitts
Sun Young Kim
Clarice de Azevedo Souza
Pierrette Geoffroy
Dimitri Heintz
Daniel Krahn
Markus Kaiser
Erich Kombrink
Thierry Heitz
Dae-Yeon Suh
Michel Legrand
Carl J Douglas
Institut de Biologie Moléculaire des Plantes · FRUniversity of Regina · CAUniversité de Strasbourg · FRUniversity of British Columbia · CAUniversity of Duisburg-Essen · DEMax Planck Institute for Plant Breeding Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant type III polyketide synthases (PKSs) catalyze the condensation of malonyl-CoA units with various CoA ester starter molecules to generate a diverse array of natural products. The fatty acyl-CoA esters synthesized by Arabidopsis thaliana ACYL-COA SYNTHETASE5 (ACOS5) are key intermediates in the biosynthesis of sporopollenin, the major constituent of exine in the outer pollen wall. By coexpression analysis, we identified two Arabidopsis PKS genes, POLYKETIDE SYNTHASE A (PKSA) and PKSB (also known as LAP6 and LAP5, respectively) that are tightly coexpressed with ACOS5. Recombinant PKSA and PKSB proteins generated tri-and tetraketide α-pyrone compounds in vitro from a broad range of potential ACOS5-generated fatty acyl-CoA starter substrates by condensation with malonyl-CoA. Furthermore, substrate preference profile and kinetic analyses strongly suggested that in planta substrates for both enzymes are midchain- and ω-hydroxylated fatty acyl-CoAs (e.g., 12-hydroxyoctadecanoyl-CoA and 16-hydroxyhexadecanoyl-CoA), which are the products of sequential actions of anther-specific fatty acid hydroxylases and acyl-CoA synthetase. PKSA and PKSB are specifically and transiently expressed in tapetal cells during microspore development in Arabidopsis anthers. Mutants compromised in expression of the PKS genes displayed pollen exine layer defects, and a double pksa pksb mutant was completely male sterile, with no apparent exine. These results show that hydroxylated α-pyrone polyketide compounds generated by the sequential action of ACOS5 and PKSA/B are potential and previously unknown sporopollenin precursors.

Indexed as

PollenAllelesArabidopsisArabidopsis ProteinsBiopolymersCarotenoidsGenes, PlantIn Situ HybridizationKineticsMicroscopy, Electron, TransmissionMutationPolyketide SynthasesRecombinant ProteinsReverse Transcriptase Polymerase Chain ReactionArabidopsis ProteinsBiopolymersCarotenoidsLAP5 protein, ArabidopsisLAP6 protein, ArabidopsisPolyketide SynthasesRecombinant Proteinssporopollenin

Identifiers

PMID21193570
PMCPMC3027170
OpenAlexW2156288299

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.