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Characterization of the nuclear proteome of Chlamydomonas reinhardtii in response to salt stress

ABSTRACT: Microalgae technology is a promising alternative feedstock for biodiesel production. Chlamydomonas reinhardtii is a unicellular green alga, one of the most important model organisms, that can produce increased lipid yields under abiotic conditions. In this study we show that treatment with 0.1 M of NaCl rapidly raises the amount of neutral lipids in C. reinhardtii, without impairing cellular growth rate, being, therefore, a favorable condition for biomass and energy production. A nuclear proteomic analysis was conducted on salt stress to better understand the molecular mechanism and the regulatory proteins involved in the adaptation to salt stress and increased lipid yields.

INSTRUMENT(S):

ORGANISM(S): Chlamydomonas Reinhardtii

TISSUE(S): Photosynthetic Cell

SUBMITTER: Flavia Vischi Winck

LAB HEAD: Flavia Vischi Winck

PROVIDER: PXD034581 | Pride | 2025-10-14

REPOSITORIES: Pride

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			Action	DRS
	PN1_1111.csv	Csv
	PN1_2-C_7_01_7123.d.zip	Other
	PN1_2-C_7_01_7123_uncalib_4.3.110.mgf	Mgf
	PN2_1211.csv	Csv
	PN2_2-E_8_01_7140.d.zip	Other

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UNASSAMBLED CELL WALL PROTEINS FORM AGGREGATES IN THE EXTRACELLULAR SPACE OF CHLAMYDOMONAS REINHARDTII STRAIN UVM4

Project description:The green microalga Chlamydomonas reinhardtii is emerging as a promising cell biofactory for secreted recombinant protein (RP) production. In recent years, the generation of the broadly-used cell wall-deficient mutant strain UVM4 has allowed for a drastic increase in secreted RP yields. However, purification of secreted RPs from the extracellular space of C. reinhardtii strain UVM4 is challenging. Previous studies suggest that secreted RPs are trapped in a matrix of cell wall protein aggregates populating the secretome of strain UVM4, making it difficult to isolate and purify the RPs. To better understand the nature and behaviour of these extracellular protein aggregates, we analysed and compared the extracellular proteome of the strain UVM4 to its cell-walled ancestor, C. reinhardtii strain 137c. When grown under the same conditions, strain UVM4 produced a unique extracellular proteomic profile, including a higher abundance of secreted cell wall glycoproteins. Further characterization of high molecular weight extracellular protein aggregates in strain UVM4 revealed that they are largely comprised of pherophorins, a specific class of cell wall glycoproteins. Our results offer important new insights into the extracellular space of strain UVM4, including strain-specific secreted cell wall proteins and the composition of the aggregates possibly related to impaired RP purification. The discovery of pherophorins as a major component of extracellular protein aggregates will inform future strategies to remove or prevent aggregate formation, enhance purification of secreted RPs, and improve yields of recombinant biopharmaceuticals in this emerging cell biofactory.

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