Heat Shock Protein HSP101 Binds to the <i>Fed-1</i> Internal Light Regulatory Element and Mediates Its High Translational Activity

Ling, Jun; Wells, Douglas R.; Tanguay, Robert L.; Dickey, Lynn F.; Thompson, William F.; Gallie, Daniel

doi:10.1105/tpc.12.7.1213

Cited by 54 publications

(23 citation statements)

References 31 publications

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“…A yeast mutant lacking HSP104 could not acquire thermotolerance [10, 11] which shows its role in the defense mechanism of plants. In addition to its role in thermotolerance, HSP101 has also been suggested to increase translation activity [12,13]. Keeping in view the roles of two proteins, it is hypothesized that they interacts and complement with each other and activates self-defense mechanism in the plants when they are exposed to high temperature.…”

Section: Introductionmentioning

confidence: 99%

Interaction Studies of Heat Shock Responsive Protein HSA32 and Heat Shock Protein HSP101: An In Silico Approach

-ur-Rahman¹

2013

PAB

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Research ArticleABSTRACT Heat shock responsive protein HSA32 is a good candidate responsible for heat stress tolerance in crop plants. It interacts with other proteins in a signaling pathway which results its regulation of gene expression in response to heat shock. HSP101 is such protein which in combination with HSA32 is essential to thermotolerance in crop plants. In this study, we constructed 3-D structures of the two proteins. Hypothetical point mutations were also induced in HSA32 protein at amino acid position 27, 91, 159 and 220 and their 3-D models were developed. Then, protein -protein interaction was studied between two proteins. Our results showed that HSA32 and HSP101 proteins interact with each other in the active binding sites. It was also found that mutants HSA32 E

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Section: Introductionmentioning

confidence: 99%

Interaction Studies of Heat Shock Responsive Protein HSA32 and Heat Shock Protein HSP101: An In Silico Approach

-ur-Rahman¹

2013

PAB

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“…In Arabidopsis, HSP101 is required for both SAT and LAT . In addition to its role in thermotolerance, HSP101 was reported to have translation-enhancing activity (Wells et al, 1998;Ling et al, 2000).…”

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confidence: 99%

Interplay between Heat Shock Proteins HSP101 and HSA32 Prolongs Heat Acclimation Memory Posttranscriptionally in Arabidopsis

Juan

Hsu

et al. 2013

Plant Physiology

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Heat acclimation improves the tolerance of organisms to severe heat stress. Our previous work showed that in Arabidopsis (Arabidopsis thaliana), the "memory" of heat acclimation treatment decayed faster in the absence of the heat-stress-associated 32-kD protein HSA32, a heat-induced protein predominantly found in plants. The HSA32 null mutant attains normal short-term acquired thermotolerance but is defective in long-term acquired thermotolerance. To further explore this phenomenon, we isolated Arabidopsis defective in long-term acquired thermotolerance (dlt) mutants using a forward genetic screen. Two recessive missense alleles, dlt1-1 and dlt1-2, encode the molecular chaperone heat shock protein101 (HSP101). Results of immunoblot analyses suggest that HSP101 enhances the translation of HSA32 during recovery after heat treatment, and in turn, HSA32 retards the decay of HSP101. The dlt1-1 mutation has little effect on HSP101 chaperone activity and thermotolerance function but compromises the regulation of HSA32. In contrast, dlt1-2 impairs the chaperone activity and thermotolerance function of HSP101 but not the regulation of HSA32. These results suggest that HSP101 has a dual function, which could be decoupled by the mutations. Pulse-chase analysis showed that HSP101 degraded faster in the absence of HSA32. The autophagic proteolysis inhibitor E-64d, but not the proteasome inhibitor MG132, inhibited the degradation of HSP101. Ectopic expression of HSA32 confirmed its effect on the decay of HSP101 at the posttranscriptional level and showed that HSA32 was not sufficient to confer long-term acquired thermotolerance when the HSP101 level was low. Taken together, we propose that a positive feedback loop between HSP101 and HSA32 at the protein level is a novel mechanism for prolonging the memory of heat acclimation.

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“…Thus, we favor the possibility that by sequence-specific binding, a factor such as a protein or metabolite interacts with the (CAUU) 4 element, possibly in combination with proteins at the 5 0 end of the mRNA to control light-responsive mRNA stability. HSP101 binds Fed-1 5 0 UTR in vitro and may be necessary for enhancing Fed-1 mRNA translation (Ling et al, 2000), although whether or not HSP101 interacts with the (CAUU) 4 repeat or affects mRNA stability is yet unclear. It is interesting to note that mammalian HSP70 and HSP110 also have been shown to bind AU-rich RNAs in vitro (Henics et al, 1999).…”

Section: Discussionmentioning

confidence: 98%

The Fed-1 (CAUU)4 element is a 5? UTR dark-responsive mRNA instability element that functions independently of dark-induced polyribosome dissociation

et al. 2004

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Darkness rapidly induces a decline in the stability and translation of the pea Ferredoxin-1 (Fed-1) mRNA in transgenic tobacco. Direct half-life measurement showed that mutation of the (CAUU)4 stabilizes Fed-1 mRNA in the dark. (CAUU)1, a feature more common in plant 5' UTRs than (CAUU)4, confers slight light-responsive mRNA accumulation. At least three but less than 11 CAUU repeats near the 5' end of the 5' UTR are required for full light-responsive accumulation. Furthermore, 26 nt of the 5' UTR, including the (CAUU)4 repeat, is sufficient to confer a significant approximately 2.5-fold increase in light-regulated mRNA accumulation when fused to the 5' end of a heterologous plant mRNA. A mutation of the (CAUU)4 repeat that compromises light-regulated mRNA stability changes in vitro the accessibility of the region to ribonuclease V1 and ribonuclease A suggesting the geometry formed by the repeat may be important for instability. Finally, dark-induced Fed-1 mRNA instability occurs even when most of the mRNA is retained on polyribosomes, and thus is likely an independent event regulated by darkness.

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Heat Shock Protein HSP101 Binds to the Fed-1 Internal Light Regulatory Element and Mediates Its High Translational Activity

Cited by 54 publications

References 31 publications

Interaction Studies of Heat Shock Responsive Protein HSA32 and Heat Shock Protein HSP101: An In Silico Approach

Interaction Studies of Heat Shock Responsive Protein HSA32 and Heat Shock Protein HSP101: An In Silico Approach

Interplay between Heat Shock Proteins HSP101 and HSA32 Prolongs Heat Acclimation Memory Posttranscriptionally in Arabidopsis

The Fed-1 (CAUU)4 element is a 5? UTR dark-responsive mRNA instability element that functions independently of dark-induced polyribosome dissociation

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