Opinion
Feeling the Heat: Searching for Plant Thermosensors

https://doi.org/10.1016/j.tplants.2018.11.004Get rights and content

Highlights

Thermosensing is the primary event in any temperature signaling pathway and is distinguished from other temperature-responsive processes.

Temperature can alter the structure of DNA, RNA, and proteins through thermodynamic effects that impact their activity/function.

Membrane fluidity is affected by temperature and may influence the activity of membrane-associated proteins.

Systematic detection of structural information and changes therein has advanced in recent years and contributed to the identification of potential thermosensors in other species.

To draw the complete picture of plant thermal signaling, it is important to find the missing links between the temperature cue, the actual sensing, and the subsequent response. In this context, several plant thermosensors have been proposed. Here, we compare these with thermosensors in various other organisms, put them in the context of thermosensing in plants, and suggest a set of criteria to which a thermosensor must adhere. Finally, we propose that more emphasis should be given to structural analysis of DNA, RNA, and proteins in light of the activity of potential thermosensors.

Section snippets

What’s in a Name: A Redefinition of Thermosensors

In recent years, various plant proteins have been shown to act as thermosensors 1, 2, 3 or have been mistakenly referred to as thermosensors [4]. While the term ‘thermosensor’ or ‘thermosensory’ has been used often, most of the described molecular regulation is limited to explaining the actual response to temperature elevation [5]. But what is a true thermosensor? For all environmental responses, sensing is the primary step during which a sensor directly decodes a stimulus into cellular

Can DNA/Chromatin Structures Function as Thermosensors?

In bacteria, DNA replication and transcription is very sensitive to DNA supercoiling (see Glossary), which is highly regulated by temperature 13, 14. Further, DNA–protein structures, such as the DNA bend created by the histone-like nucleoid-structuring (H-NS) protein, can melt and allow the transcription of the virulence-regulating transcription factor virF and host invasion at the critical threshold temperature of 32°C [15].

In Arabidopsis, in response to increased temperature (above 22°C), the

RNA Thermosensors in Plants: An Unexplored Territory

RNA secondary structures regulate many RNA-related processes and such structures are sensitive to environmental changes [21]. In bacteria, some mRNA stem-loop structures can be ‘unzipped’ by high temperature, facilitating ribosome binding and translation (Figure 2B) [22]. In addition to RNA zippers, RNA can also adopt distinct stem-loop structures at different temperatures (RNA switches) that play a role in translational regulation [22]. RNA-mediated thermosensing has also been described in

What about Thermosensors for Alternative Splicing?

Alternative splicing affected by temperature has been observed frequently in plants (Figure 2C) [29]. A well-known example is the alternative splicing of pre-mRNA of FLOWERING LOCUS M (FLM), resulting in a temperature-dependent ratio of two isoforms, FLM-β and FLM-δ, where the FLM-β level mainly contributes to thermoresponsive flowering 30, 31, 32. However, the thermosensing components for this response remain unknown.

RNA secondary structures play an important role in RNA splicing regulation 29

Thermosensing via Protein Conformational Changes

Temperature may directly influence the activity of proteins. For example, the reaction rate of an enzymatic reaction increases to an optimal temperature due to the higher kinetic energy, which leads to more enzyme–substrate contacts, whereas excessively high temperature disturbs protein folding and activity [43]. In addition, proteins are dynamic structures which can be highly influenced by changes in temperature (Figure 2D) [44]. Hence, conformational changes can serve as mechanisms for direct

What about Thermosensing at the Membrane?

Besides intrinsic thermal sensitivity, in some cases, protein conformational changes are coupled to a temperature-induced change of the biochemical environment in which the protein resides. For example, membrane-associated proteins need to adapt their conformation so that their transmembrane part maintains an optimal hydrophobic contact with the lipid bilayer surrounding it (Figure 2F) [58]. Noticeably, the fluidity of the lipid bilayer is highly affected by temperature [59] and can function as

Concluding Remarks and Future Perspectives

Collectively, we would like to propose a set of criteria to which a thermosensor has to adhere (Figure 1): (1) one or several properties (such as structural features or activity) of a thermosensor need to be directly altered by temperature changes; (2) these properties are important for the functional module(s) in which the thermosensor participates and need to be efficiently and reproducibly interpreted to convey the temperature information to the response machineries; and (3) the

Acknowledgements

L.D.V is a recipient of the VIB International PhD Scholarship in Life Sciences.

Glossary

Alternative splicing
after transcription, in eukaryotes, the pre-mature mRNA undergoes splicing to remove introns. However, in some cases, introns will be retained in the mature mRNA or exons will be removed to finally generate different protein isoforms that may have different functions.
DNA supercoiling
this DNA topology can be created by over- or underwinding of the DNA double strand. Supercoiling can be lifted by topoisomerases that are specific for different types of supercoiling, a process

References (79)

  • Z. Török

    Plasma membranes as heat stress sensors: from lipid-controlled molecular switches to therapeutic applications

    Biochim. Biophys. Acta Biomembr.

    (2014)
  • T.F. Martin

    PI(4,5)P2 regulation of surface membrane traffic

    Curr. Opin. Cell Biol.

    (2001)
  • B.J. Grant

    Large conformational changes in proteins: signaling and other functions

    Curr. Opin. Struct. Biol.

    (2010)
  • Y. Fujii

    Phototropin perceives temperature based on the lifetime of its photoactivated state

    Proc. Natl. Acad. Sci. U. S. A.

    (2017)
  • J.-H. Jung

    Phytochromes function as thermosensors in Arabidopsis

    Science

    (2016)
  • M. Legris

    Phytochrome B integrates light and temperature signals in Arabidopsis

    Science

    (2016)
  • D. Coleman-Derr et al.

    Deposition of histone variant H2A.Z within gene bodies regulates responsive genes

    PLoS Genet.

    (2012)
  • M. Quint

    Molecular and genetic control of plant thermomorphogenesis

    Nat. Plants

    (2016)
  • N.C. Rockwell

    Phytochrome structure and signaling mechanisms

    Annu. Rev. Plant Biol.

    (2006)
  • S.V. Kumar

    Transcription factor PIF4 controls the thermosensory activation of flowering

    Nature

    (2012)
  • C.A. Reynolds

    Free energy calculations in molecular biophysics

    Mol. Phys.

    (1992)
  • E.F. Markovskaya et al.

    Low temperature sensors in plants: hypotheses and assumptions

    Biol. Bull.

    (2017)
  • T. Mizushima

    Increase in negative supercoiling of plasmid DNA in Escherichia coli exposed to cold shock

    Mol. Microbiol.

    (1997)
  • M. Falconi

    Thermoregulation of Shigella and Escherichia coli EIEC pathogenicity. A temperature-dependent structural transition of DNA modulates accessibility of virF promoter to transcriptional repressor H-NS

    EMBO J.

    (1998)
  • W. Sura

    Dual role of the histone variant H2A.Z in transcriptional regulation of stress-response genes

    Plant Cell

    (2017)
  • C. Tasset

    POWERDRESS-mediated histone deacetylation is essential for thermomorphogenesis in Arabidopsis thaliana

    PLoS Genet.

    (2018)
  • L.E. Vandivier

    The conservation and function of RNA secondary structure in plants

    Annu. Rev. Plant Biol.

    (2016)
  • J. Kortmann et al.

    Bacterial RNA thermometers: molecular zippers and switches

    Nat. Rev. Microbiol.

    (2012)
  • I. Shamovsky

    RNA-mediated response to heat shock in mammalian cells

    Nature

    (2006)
  • E. Yángüez

    Analysis of genome-wide changes in the translatome of Arabidopsis seedlings subjected to heat stress

    PLoS One

    (2013)
  • M.V. Grosso-Becerra

    Regulation of Pseudomonas aeruginosa virulence factors by two novel RNA thermometers

    Proc. Natl. Acad. Sci. U. S. A.

    (2014)
  • X. Yang

    New era of studying RNA secondary structure and its influence on gene regulation in plants

    Front. Plant Sci.

    (2018)
  • F. Righetti

    Temperature-responsive in vitro RNA structurome of Yersinia pseudotuberculosis

    Proc. Natl. Acad. Sci. U. S. A.

    (2016)
  • Y. Ding

    In vivo genome-wide profiling of RNA secondary structure reveals novel regulatory features

    Nature

    (2014)
  • U. Lutz

    Natural haplotypes of FLM non-coding sequences fine-tune flowering time in ambient spring temperatures in Arabidopsis

    eLife

    (2017)
  • D. Posé

    Temperature-dependent regulation of flowering by antagonistic FLM variants

    Nature

    (2013)
  • S. Sureshkumar

    Nonsense-mediated mRNA decay modulates FLM-dependent thermosensory flowering response in Arabidopsis

    Nat. Plants

    (2016)
  • P.J. Shepard et al.

    Conserved RNA secondary structures promote alternative splicing

    RNA

    (2008)
  • A.B. James

    Global spatial analysis of Arabidopsis natural variants implicates 5′UTR splicing of LATE ELONGATED HYPOCOTYL in responses to temperature

    Plant Cell Environ.

    (2018)
  • Cited by (0)

    View full text