The plastid proteome of the nonphotosynthetic chlorophycean alga Polytomella parva

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The plastid proteome of the nonphotosynthetic chlorophycean alga Polytomella parva. / Fuentes-Ramírez, Emma O; Vázquez-Acevedo, Miriam; Cabrera-Orefice, Alfredo; Guerrero-Castillo, Sergio; González-Halphen, Diego.

In: MICROBIOL RES, Vol. 243, 02.2021, p. 126649.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

Harvard

Fuentes-Ramírez, EO, Vázquez-Acevedo, M, Cabrera-Orefice, A, Guerrero-Castillo, S & González-Halphen, D 2021, 'The plastid proteome of the nonphotosynthetic chlorophycean alga Polytomella parva', MICROBIOL RES, vol. 243, pp. 126649. https://doi.org/10.1016/j.micres.2020.126649

APA

Fuentes-Ramírez, E. O., Vázquez-Acevedo, M., Cabrera-Orefice, A., Guerrero-Castillo, S., & González-Halphen, D. (2021). The plastid proteome of the nonphotosynthetic chlorophycean alga Polytomella parva. MICROBIOL RES, 243, 126649. https://doi.org/10.1016/j.micres.2020.126649

Vancouver

Bibtex

@article{14e7b8c384de4bdc91c4dd77df8b7090,
title = "The plastid proteome of the nonphotosynthetic chlorophycean alga Polytomella parva",
abstract = "The unicellular, free-living, nonphotosynthetic chlorophycean alga Polytomella parva, closely related to Chlamydomonas reinhardtii and Volvox carteri, contains colorless, starch-storing plastids. The P. parva plastids lack all light-dependent processes but maintain crucial metabolic pathways. The colorless alga also lacks a plastid genome, meaning no transcription or translation should occur inside the organelle. Here, using an algal fraction enriched in plastids as well as publicly available transcriptome data, we provide a morphological and proteomic characterization of the P. parva plastid, ultimately identifying several plastid proteins, both by mass spectrometry and bioinformatic analyses. Data are available via ProteomeXchange with identifier PXD022051. Altogether these results led us to propose a plastid proteome for P. parva, i.e., a set of proteins that participate in carbohydrate metabolism; in the synthesis and degradation of starch, amino acids and lipids; in the biosynthesis of terpenoids and tetrapyrroles; in solute transport and protein translocation; and in redox homeostasis. This is the first detailed plastid proteome from a unicellular, free-living colorless alga.",
keywords = "Amino Acids/metabolism, Chlorophyta/chemistry, Genome, Plastid, Mass Spectrometry, Plastids/chemistry, Proteome/chemistry, Proteomics",
author = "Fuentes-Ram{\'i}rez, {Emma O} and Miriam V{\'a}zquez-Acevedo and Alfredo Cabrera-Orefice and Sergio Guerrero-Castillo and Diego Gonz{\'a}lez-Halphen",
note = "Copyright {\textcopyright} 2020. Published by Elsevier GmbH.",
year = "2021",
month = feb,
doi = "10.1016/j.micres.2020.126649",
language = "English",
volume = "243",
pages = "126649",
journal = "MICROBIOL RES",
issn = "0944-5013",
publisher = "Urban und Fischer Verlag Jena",

}

RIS

TY - JOUR

T1 - The plastid proteome of the nonphotosynthetic chlorophycean alga Polytomella parva

AU - Fuentes-Ramírez, Emma O

AU - Vázquez-Acevedo, Miriam

AU - Cabrera-Orefice, Alfredo

AU - Guerrero-Castillo, Sergio

AU - González-Halphen, Diego

N1 - Copyright © 2020. Published by Elsevier GmbH.

PY - 2021/2

Y1 - 2021/2

N2 - The unicellular, free-living, nonphotosynthetic chlorophycean alga Polytomella parva, closely related to Chlamydomonas reinhardtii and Volvox carteri, contains colorless, starch-storing plastids. The P. parva plastids lack all light-dependent processes but maintain crucial metabolic pathways. The colorless alga also lacks a plastid genome, meaning no transcription or translation should occur inside the organelle. Here, using an algal fraction enriched in plastids as well as publicly available transcriptome data, we provide a morphological and proteomic characterization of the P. parva plastid, ultimately identifying several plastid proteins, both by mass spectrometry and bioinformatic analyses. Data are available via ProteomeXchange with identifier PXD022051. Altogether these results led us to propose a plastid proteome for P. parva, i.e., a set of proteins that participate in carbohydrate metabolism; in the synthesis and degradation of starch, amino acids and lipids; in the biosynthesis of terpenoids and tetrapyrroles; in solute transport and protein translocation; and in redox homeostasis. This is the first detailed plastid proteome from a unicellular, free-living colorless alga.

AB - The unicellular, free-living, nonphotosynthetic chlorophycean alga Polytomella parva, closely related to Chlamydomonas reinhardtii and Volvox carteri, contains colorless, starch-storing plastids. The P. parva plastids lack all light-dependent processes but maintain crucial metabolic pathways. The colorless alga also lacks a plastid genome, meaning no transcription or translation should occur inside the organelle. Here, using an algal fraction enriched in plastids as well as publicly available transcriptome data, we provide a morphological and proteomic characterization of the P. parva plastid, ultimately identifying several plastid proteins, both by mass spectrometry and bioinformatic analyses. Data are available via ProteomeXchange with identifier PXD022051. Altogether these results led us to propose a plastid proteome for P. parva, i.e., a set of proteins that participate in carbohydrate metabolism; in the synthesis and degradation of starch, amino acids and lipids; in the biosynthesis of terpenoids and tetrapyrroles; in solute transport and protein translocation; and in redox homeostasis. This is the first detailed plastid proteome from a unicellular, free-living colorless alga.

KW - Amino Acids/metabolism

KW - Chlorophyta/chemistry

KW - Genome, Plastid

KW - Mass Spectrometry

KW - Plastids/chemistry

KW - Proteome/chemistry

KW - Proteomics

U2 - 10.1016/j.micres.2020.126649

DO - 10.1016/j.micres.2020.126649

M3 - SCORING: Journal article

C2 - 33285428

VL - 243

SP - 126649

JO - MICROBIOL RES

JF - MICROBIOL RES

SN - 0944-5013

ER -