Differential expression profiling of heat stressed tardigrades reveals major shift in the transcriptome.


Journal

Comparative biochemistry and physiology. Part A, Molecular & integrative physiology
ISSN: 1531-4332
Titre abrégé: Comp Biochem Physiol A Mol Integr Physiol
Pays: United States
ID NLM: 9806096

Informations de publication

Date de publication:
05 2022
Historique:
received: 28 12 2021
revised: 14 02 2022
accepted: 14 02 2022
pubmed: 20 2 2022
medline: 6 5 2022
entrez: 19 2 2022
Statut: ppublish

Résumé

Tardigrades are renowned for their extreme stress tolerance, which includes the ability to endure complete desiccation, high levels of radiation and very low sub-zero temperatures. Nevertheless, tardigrades appear to be vulnerable to high temperatures and thus the potential effects of global warming. Here, we provide the first analysis of transcriptome data obtained from heat stressed specimens of the eutardigrade Ramazzottius varieornatus, with the aim of providing new insights into the molecular processes affected by high temperatures. Specifically, we compare RNA-seq datasets obtained from active, heat-exposed (35 °C) tardigrades to that of active controls kept at 5 °C. Our data reveal a surprising shift in transcription, involving 9634 differentially expressed transcripts, corresponding to >35% of the transcriptome. The latter data are in striking contrast to the hitherto observed constitutive expression underlying tardigrade extreme stress tolerance and entrance into the latent state of life, known as cryptobiosis. Thus, when examining the molecular response, heat-stress appears to be more stressful for R. varieornatus than extreme conditions, such as desiccation or freezing. A gene ontology analysis reveals that the heat stress response involves a change in transcription and presumably translation, including an adjustment of metabolism, and, putatively, preparation for encystment and subsequent diapause. Among the differentially expressed transcripts we find heat-shock proteins as well as the eutardigrade specific proteins (CAHS, SAHS, MAHS, RvLEAM, and Dsup). The latter proteins thus seem to contribute to a general stress response, and may not be directly related to cryptobiosis.

Identifiants

pubmed: 35182765
pii: S1095-6433(22)00027-7
doi: 10.1016/j.cbpa.2022.111169
pii:
doi:

Substances chimiques

Heat-Shock Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

111169

Commentaires et corrections

Type : ErratumIn

Informations de copyright

Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.

Auteurs

Ricardo Cardoso Neves (RC)

Department of Biology, University of Copenhagen, Copenhagen, Denmark.

Ask Møbjerg (A)

Center for Evolutionary Hologenomics, The Globe Institute, University of Copenhagen, Copenhagen, Denmark.

Miyako Kodama (M)

Center for Evolutionary Hologenomics, The Globe Institute, University of Copenhagen, Copenhagen, Denmark.

Jazmín Ramos-Madrigal (J)

Center for Evolutionary Hologenomics, The Globe Institute, University of Copenhagen, Copenhagen, Denmark.

M Thomas P Gilbert (MTP)

Center for Evolutionary Hologenomics, The Globe Institute, University of Copenhagen, Copenhagen, Denmark; University Museum, NTNU, Trondheim, Norway.

Nadja Møbjerg (N)

Department of Biology, University of Copenhagen, Copenhagen, Denmark. Electronic address: nmobjerg@bio.ku.dk.

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Classifications MeSH