A ubiquitinome and proteome dataset of the red alga Gracilariopsis lemaneiformis under cold stress.
4 affiliations
- 1Key Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Qingdao, 266003, Shandong, China.
- 2Marine Science Institute, Shantou University, Shantou, 515063, China. [email protected].
- 3Guangdong Provincial Key Laboratory of Marine Biotechnology, Shantou University, Shantou, 515063, China. [email protected].
- 4Key Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Qingdao, 266003, Shandong, China. [email protected].
Abstract
Low temperature is a major environmental factor constraining the growth and aquaculture performance of the red alga Gracilariopsis lemaneiformis, yet systematic protein-level data describing cold stress responses remain limited. Ubiquitination is a key post-translational modification involved in regulating protein stability and turnover during stress adaptation. Here, we present a paired dataset of the global proteome and the ubiquitin-modified proteome of G. lemaneiformis under cold stress, generated using a matched experimental design across identical conditions. This paired dataset provides a valuable resource for future investigations of the relationship between protein abundance changes and ubiquitination regulation during cold-stress responses. We further provide detailed technical validation demonstrating high data quality and strong reproducibility among biological replicates. These datasets constitute a valuable resource for investigating ubiquitination-associated protein homeostasis during cold adaptation, facilitating the identification of ubiquitination-regulated substrate candidates under cold stress, and supporting downstream functional studies as well as the breeding of cold-tolerant G. lemaneiformis strains.
Related
- De novo transcriptome of the red alga Gracilariopsis tenuifrons (Gracilariales, Rhodophyta) in response to prolonged temperature stress
- Ubiquitinome dynamics and regulation by DUB2 during Leishmania differentiation
- Dark proteome ensemble superposition gating calibrates biosynthesis of antiviral cocktail
- Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins
- Direct aliquoting from a single heated well enables fully automated high-throughput thermal proteome profiling
BibTeX
@article{qin2026ubiquitinome,
title = {{A ubiquitinome and proteome dataset of the red alga Gracilariopsis lemaneiformis under cold stress.}},
author = {Feng Qin and Xiuyu Zhang and Shuangshuang Peng and Jianxin Sun and Di Xu and Weizhou Chen and Xiaonan Zang},
journal = {Scientific data},
year = {2026},
month = oct,
doi = {10.1038/s41597-026-07789-w},
url = {https://europepmc.org/article/MED/42897193},
note = {CC BY},
}
RIS
TY - JOUR
TI - A ubiquitinome and proteome dataset of the red alga Gracilariopsis lemaneiformis under cold stress.
AU - Feng Qin
AU - Xiuyu Zhang
AU - Shuangshuang Peng
AU - Jianxin Sun
AU - Di Xu
AU - Weizhou Chen
AU - Xiaonan Zang
PY - 2026
DA - 2026/10/19
JO - Scientific data
DO - 10.1038/s41597-026-07789-w
UR - https://europepmc.org/article/MED/42897193
AB - Low temperature is a major environmental factor constraining the growth and aquaculture performance of the red alga Gracilariopsis lemaneiformis, yet systematic protein-level data describing cold stress responses remain limited. Ubiquitination is a key post-translational modification involved in regulating protein stability and turnover during stress adaptation. Here, we present a paired dataset of the global proteome and the ubiquitin-modified proteome of G. lemaneiformis under cold stress, generated using a matched experimental design across identical conditions. This paired dataset provides a valuable resource for future investigations of the relationship between protein abundance changes and ubiquitination regulation during cold-stress responses. We further provide detailed technical validation demonstrating high data quality and strong reproducibility among biological replicates. These datasets constitute a valuable resource for investigating ubiquitination-associated protein homeostasis during cold adaptation, facilitating the identification of ubiquitination-regulated substrate candidates under cold stress, and supporting downstream functional studies as well as the breeding of cold-tolerant G. lemaneiformis strains.
SN - 2052-4463
ER -