Proteomics

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Dynamic regulation of the proteome and lysine acetylome of Chlamydomonas reinhardtii in dependence on light and acetate


ABSTRACT: Here, we performed a mass spectrometry-based analysis to study lysine acetylation and proteome dynamics in Chlamydomonas under varying growth conditions. Liquid cultures of Chlamydomonas were transferred from mixotrophic (light and acetate as carbon source) to heterotrophic (dark and acetate), or photoautotrophic (light only) growth conditions for 30 h before harvest. The proteome and acetylome changes between the different growth conditions were quantified using a stable isotope based dimethyl-labelling technique. The presence of lysine acetylation on nearly all enzymes involved in the glyoxylate cycle and its dynamic regulation in dependence on acetate was one of the major results of this study. Our results clearly show that lysine acetylation is dynamically regulated in Chlamydomonas in dependence on light and acetate. Furthermore, the newly identified lysine acetylation sites have a great potential for genetic engineering of metabolic pathways in Chlamydomonas.

ORGANISM(S): Chlamydomonas Reinhardtii

SUBMITTER: Iris Finkemeier 

PROVIDER: PXD025168 | JPOST Repository | Fri Nov 19 00:00:00 GMT 2021

REPOSITORIES: jPOST

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Dynamic light- and acetate-dependent regulation of the proteome and lysine acetylome of Chlamydomonas.

Füßl Magdalena M   König Ann-Christine AC   Eirich Jürgen J   Hartl Markus M   Kleinknecht Laura L   Bohne Alexandra-Viola AV   Harzen Anne A   Kramer Katharina K   Leister Dario D   Nickelsen Jörg J   Finkemeier Iris I  

The Plant journal : for cell and molecular biology 20211118 1


The green alga Chlamydomonas reinhardtii is one of the most studied microorganisms in photosynthesis research and for biofuel production. A detailed understanding of the dynamic regulation of its carbon metabolism is therefore crucial for metabolic engineering. Post-translational modifications can act as molecular switches for the control of protein function. Acetylation of the ɛ-amino group of lysine residues is a dynamic modification on proteins across organisms from all kingdoms. Here, we per  ...[more]

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