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Planta

, Volume 250, Issue 5, pp 1449–1460 | Cite as

AtJ3, a specific HSP40 protein, mediates protein farnesylation-dependent response to heat stress in Arabidopsis

  • Jia-Rong Wu
  • Tzu-Yun Wang
  • Chi-Pei Weng
  • Ngoc Kieu Thi Duong
  • Shaw-Jye WuEmail author
Original Article

Abstract

Main conclusion

Despite AtJ3 and AtJ2 sharing a high protein-sequence identity and both being substrates of protein farnesyltransferase (PFT), AtJ3 but not AtJ2 mediates in Arabidopsis the heat-dependent phenotypes derived from farnesylation modification.

Abstract

Arabidopsis HEAT-INTOERANT 5 (HIT5)/ENHANCED RESPONSE TO ABA 1 (ERA1) encodes the β-subunit of the protein farnesyltransferase (PFT), and the hit5/era1 mutant is better able to tolerate heat-shock stress than the wild type. Given that Arabidopsis AtJ2 (J2) and AtJ3 (J3) are heat-shock protein 40 (HSP40) homologs, sharing 90% protein-sequence identity, and each contains a CaaX box for farnesylation; atj2 (j2) and atj3 (j3) mutants were subjected to heat-shock treatment. Results showed that j3 but not j2 manifested the heat-shock tolerant phenotype. In addition, transgenic j3 plants that expressed a CaaX- abolishing J3C417S construct maintained the same capacity to tolerate heat shock as j3. The basal transcript levels of HEAT-SHOCK PROTEIN 101 (HSP101) in hit5/era1 and j3 were higher than those in the wild type. Although the capacities of j3/hsp101 and hit5/hsp101 double mutants to tolerate heat-shock stress declined compared to those of j3 and hit5/era1, they were still greater than that of the wild type. These results show that a lack of farnesylated J3 contributes to the heat-dependent phenotypes of hit5/era1, in part by the modulation of HSP101 activity, and also indicates that (a) mediator(s) other than J3 is (are) involved in the PFT-regulated heat-stress response. In addition, because HSP40s are known to function in dimer formation, bimolecular fluorescence complementation experiments were performed, and results show that J3 could dimerize regardless of farnesylation. In sum, in this study, a specific PFT substrate was identified, and its roles in the farnesylation-regulated heat-stress responses were clarified, which could be of use in future agricultural applications.

Keywords

DnaJ ENHANCED RESPONSE TO ABA 1 (ERA1HEAT-INTOLERANT 5 (HIT5Heat shock Heat-shock protein 40 (HSP40) Heat-shock protein 101 (HSP101) J protein Protein farnesyltransferase (PFT) 

Abbreviations

BiFC

Bi-molecular fluorescence complementation

ERA1

Enhanced response to aba 1

EYFP

Enhanced yellow fluorescence protein

HIT5

Heat-intolerant 5

HSP (40, 70, 101)

Heat-shock protein (40, 70, 101)

HSR

Heat-stress response

J2/J3

AtJ2/AtJ3 (Arabidopsis thaliana DnaJ homologue 2/3)

PFT

Protein farnesyltransferase

Notes

Acknowledgements

The authors are very grateful to Dr. Peter Brodersen for providing the J3C417S transgenic line. This work was funded by the Ministry of Science and Technology, Taiwan (MOST 105-2311-B-008-004-MY3 and 108-2311-B-008-004-MY3 to S-JW).

Supplementary material

425_2019_3239_MOESM1_ESM.pdf (688 kb)
Supplementary material 1 (PDF 688 kb)

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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Department of Life SciencesNational Central UniversityTaoyuan CityTaiwan

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