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Synergism between the chaperone-like activity of the stress regulated ASR1 protein and the osmolyte glycine-betaine

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Abstract

Abiotic stress may result in protein denaturation. To confront protein inactivation, plants activate protective mechanisms that include chaperones and chaperone-like proteins, and low-molecular weight organic molecules, known as osmolytes or compatible solutes. If these protective processes fail, the irreversibly damaged proteins are targeted for degradation. Tomato ASR1 (SlASR1) is encoded by a plant-specific gene. Steady state levels of transcripts and protein are transiently induced by salt and water stress in an ABA-dependent manner. SlASR1 is localized in both the cytosol as unstructured monomers and in the nucleus as structured DNA-bound dimers. We show here that the unstructured form of SlASR1 has chaperone-like activity and can stabilize a number of proteins against denaturation caused by heat and freeze-thaw cycles. The protective activity of SlASR1 is synergistic with that of the osmolyte glycine-betaine, which accumulates under stress conditions. We suggest that the cytosolic pool of ASR1 protects proteins from denaturation.

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Abbreviations

ANS:

1-Anilinonaphthalene-8-sulphonate

ASR1:

Abscisic acid stress ripening 1

BSA:

Bovine serum albumin

CS:

Porcine muscle citrate synthase

DTT:

Dithiothreitol

Hsp:

Heat shock proteins

LDH:

Rabbit muscle lactate dehydrogenase

LEA:

Late embryogenesis abundant

SlASR1:

Tomato ASR1

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  1. Department of Life Sciences and The Doris and Bertie Black Center for Bioenergetics in Life Sciences, Ben-Gurion University of the Negev, 84105, Beer-Sheva, Israel

    Zvia Konrad & Dudy Bar-Zvi

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  1. Zvia Konrad
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  2. Dudy Bar-Zvi
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Correspondence to Dudy Bar-Zvi.

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Konrad, Z., Bar-Zvi, D. Synergism between the chaperone-like activity of the stress regulated ASR1 protein and the osmolyte glycine-betaine. Planta 227, 1213–1219 (2008). https://doi.org/10.1007/s00425-008-0693-5

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  • DOI: https://doi.org/10.1007/s00425-008-0693-5

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