PXD056333-1

PXD056333 is an original dataset announced via ProteomeXchange.

Title	Proteomic and phosphoproteomic analysis of a Haematococcus pluvialis (Chlorophyceae) mutant with a higher heterotrophic cell division rate reveals altered pathways involved in cell proliferation and nutrient partitioning
Description	Haematococcus pluvialis has been used to produce the ketocarotenoid antioxidant, astaxanthin. Currently, heterotrophic cultivation of H. pluvialis is limited by slow growth rates. This work aims to address this challenge by exploring the mechanisms of acetate metabolism in Haematococcus. Chemical mutagenesis and screening identified H. pluvialis strain KREMS 23D-3 that achieved up to a 34.9% higher cell density than the wild type when grown heterotrophically on acetate. An integrative proteomics and phosphoproteomics approach was employed to quantify 4,955 proteins and 5,099 phosphorylation sites from 2,505 phosphoproteins in the wild-type and mutant strains of H. pluvialis. Among them, 12 proteins were significantly upregulated and 22 significantly downregulated in the mutant while phosphoproteomic analysis identified 143 significantly upregulated phosphorylation sites on 106 proteins and 130 downregulated phosphorylation sites on 114 proteins. Upregulation of anaphase promoting complex phosphoproteins and downregulation of a putative cell cycle division 20 phosphoprotein in the mutant suggests rapid mitotic progression, coinciding with higher cell division rates. Upregulated coproporphyrinogen oxidase and phosphorylated magnesium chelatase in the mutant demonstrated altered nitrogen partitioning towards chlorophyll biosynthesis. The large proportion of differentially expressed phosphoproteins suggests phosphorylation is a key regulator for protein expression and activity in Haematococcus. Taken together, this study reveals the regulation of interrelated acetate metabolic pathways in H. pluvialis and provides protein targets that may guide future strain engineering work.
HostingRepository	PRIDE
AnnounceDate	2024-11-20
AnnouncementXML	Submission_2024-11-20_12:21:10.663.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD056333
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Kyarii Ramarui
SpeciesList	scientific name: Haematococcus lacustris; NCBI TaxID: 44745;
ModificationList	phosphorylated residue; acetylated residue; deamidated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2024-09-27 11:39:04	ID requested
⏵ 1	2024-11-20 12:21:11	announced

Ramarui K, Zhong J, Li Y, Proteomic and phosphoproteomic analysis of a Haematococcus pluvialis (Chlorophyceae) mutant with a higher heterotrophic cell division rate reveals altered pathways involved in cell proliferation and nutrient partitioning. J Phycol, 60(5):1173-1189(2024) [pubmed]

10.6019/PXD056333;

10.1111/jpy.13490;

submitter keyword: proteomics, post-translational modification,Cell cycle control, phosphoproteomics, chlorophyll biosynthesis, heterotrophy

Dr. Yantao Li
contact affiliation	University of Maryland Center for Environmental Science -- Institute of Marine and Environmental Technology, University of Maryland, Baltimore County
contact email	yantao@umces.edu
lab head
Kyarii Ramarui
contact affiliation	University of Maryland Center for Environmental Science -- Institute of Marine and Environmental Technology
contact email	kramarui@umces.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD056333
     1. Label: PRIDE project
     2. Name: Proteomic and phosphoproteomic analysis of a Haematococcus pluvialis (Chlorophyceae) mutant with a higher heterotrophic cell division rate reveals altered pathways involved in cell proliferation and nutrient partitioning