Docking of acetyl-CoA carboxylase to the plastid envelope membrane attenuates fatty acid production in plants (Q104064408)

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9 December 2020

title

Docking of acetyl-CoA carboxylase to the plastid envelope membrane attenuates fatty acid production in plants (English)

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9 December 2020

3

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9 December 2020

Loic Lepiniec

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9 December 2020

Steven R Van Doren

6

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9 December 2020

Sébastien Baud

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9 December 2020

Jay J Thelen

8

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9 December 2020

author name string

Yajin Ye

1

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9 December 2020

Krisztina Nikovics

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9 December 2020

Eric T Fedosejevs

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publication date

3 December 2020

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9 December 2020

published in

Nature Communications

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volume

11

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issue

1

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page(s)

6191

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Metabolic engineering of fatty acid biosynthesis in plants.

9 December 2020

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Dynamic Remodeling of the Plastid Envelope Membranes - A Tool for Chloroplast Envelope in vivo Localizations

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Import of a new chloroplast inner envelope protein is greatly stimulated by potassium phosphate

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The pea chloroplast membrane-associated protein, IEP96, is a subunit of acetyl-CoA carboxylase

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The multisubunit acetyl-CoA carboxylase is strongly associated with the chloroplast envelope through non-ionic interactions to the carboxyltransferase subunits

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WRINKLED1 encodes an AP2/EREB domain protein involved in the control of storage compound biosynthesis in Arabidopsis.

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An AP2-type transcription factor, WRINKLED1, of Arabidopsis thaliana binds to the AW-box sequence conserved among proximal upstream regions of genes involved in fatty acid synthesis.

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Identifiers

DOI

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9 December 2020

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9 December 2020

PubMed publication ID

33273474

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