The <i>Arabidopsis thaliana</i> trehalase is a plasma membrane‐bound enzyme with extracellular activity

Frison, Mathieu; Parrou, Jean-Luc; Guillaumot, Damien; Masquelier, Danièle; François, Jean; Chaumont, François; Batoko, Henri

doi:10.1016/j.febslet.2007.07.036

Cited by 49 publications

(37 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1A). The absence of the AtTRE1 protein in wild-type rosettes is in conflict with previous immunoblots showing a faint signal of AtTRE1 in rosette leaves of bolted wild-type plants (Frison et al, 2007). The antibody used in that work was raised against two peptides of the AtTRE1 protein (residues 93-107 and 377-392), while our antibody was raised against one peptide (residues 94-107).…”

Section: Isolation and Characterization Of Arabidopsis Plants With Alcontrasting

confidence: 50%

“…The protein is known to contain potential N-glycosylation sites, indicating that the enzyme might be secreted (Frison et al, 2007). GFP studies confirmed that AtTRE1 is an apoplastic enzyme anchored to the cell membrane through a putative N-terminal transmembrane span (residues 46-63; Frison et al, 2007). This finding suggests that endogenous trehalose has to be transported out of the cell in order to be degraded.…”

supporting

confidence: 48%

“…uwa.edu.au/; Heazlewood et al, 2007). The protein is known to contain potential N-glycosylation sites, indicating that the enzyme might be secreted (Frison et al, 2007). GFP studies confirmed that AtTRE1 is an apoplastic enzyme anchored to the cell membrane through a putative N-terminal transmembrane span (residues 46-63; Frison et al, 2007).…”

mentioning

confidence: 73%

“…The antibody used in that work was raised against two peptides of the AtTRE1 protein (residues 93-107 and 377-392), while our antibody was raised against one peptide (residues 94-107). It might thus be possible that our antibody, which recognizes a single epitope of AtTRE1 in close proximity to the transmembrane span, is less efficient in reaching its target than the antibody used by Frison et al (2007).…”

Section: Isolation and Characterization Of Arabidopsis Plants With Almentioning

confidence: 99%

“…The Arabidopsis trehalase, AtTRE1, can functionally replace the acid trehalase of yeast (ScAth1) when expressed in the yeast ath1D strain (Müller et al, 2001a;Frison et al, 2007). Based on in silico analysis, AtTRE1 is predicted to be localized to the extracellular space, mitochondria, or plastids (http://suba.plantenergy.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Overexpression of the Trehalase Gene AtTRE1 Leads to Increased Drought Stress Tolerance in Arabidopsis and Is Involved in Abscisic Acid-Induced Stomatal Closure

Houtte¹,

Vandesteene²,

et al. 2013

View full text Add to dashboard Cite

Introduction of microbial trehalose biosynthesis enzymes has been reported to enhance abiotic stress resistance in plants but also resulted in undesirable traits. Here, we present an approach for engineering drought stress tolerance by modifying the endogenous trehalase activity in Arabidopsis (Arabidopsis thaliana). AtTRE1 encodes the Arabidopsis trehalase, the only enzyme known in this species to specifically hydrolyze trehalose into glucose. AtTRE1-overexpressing and Attre1 mutant lines were constructed and tested for their performance in drought stress assays. AtTRE1-overexpressing plants had decreased trehalose levels and recovered better after drought stress, whereas Attre1 mutants had elevated trehalose contents and exhibited a drought-susceptible phenotype. Leaf detachment assays showed that Attre1 mutants lose water faster than wild-type plants, whereas AtTRE1-overexpressing plants have a better water-retaining capacity. In vitro studies revealed that abscisic acidmediated closure of stomata is impaired in Attre1 lines, whereas the AtTRE1 overexpressors are more sensitive toward abscisic acid-dependent stomatal closure. This observation is further supported by the altered leaf temperatures seen in trehalase-modified plantlets during in vivo drought stress studies. Our results show that overexpression of plant trehalase improves drought stress tolerance in Arabidopsis and that trehalase plays a role in the regulation of stomatal closure in the plant drought stress response.

show abstract

Section: Isolation and Characterization Of Arabidopsis Plants With Alcontrasting

confidence: 50%

supporting

confidence: 48%

mentioning

confidence: 73%

Section: Isolation and Characterization Of Arabidopsis Plants With Almentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Overexpression of the Trehalase Gene AtTRE1 Leads to Increased Drought Stress Tolerance in Arabidopsis and Is Involved in Abscisic Acid-Induced Stomatal Closure

Houtte¹,

Vandesteene²,

et al. 2013

View full text Add to dashboard Cite

show abstract

MOLECULAR CHARACTERIZATION OF SOLUBLE AND MEMBRANE‐BOUND TREHALASES OF THE WHITEFLY, Bemisia tabaci

Wang

Yan

et al. 2014

Arch Insect Biochem Physiol

View full text Add to dashboard Cite

Trehalases (Tres) have been demonstrated to be the key enzymes that are involved in various trehalose-associated physiological processes in insects. However, little attention has been devoted to the Tres in the whitefly, Bemisia tabaci. In this study, a soluble Tre (BtTre-1) and a membrane-bound Tre (BtTre-2) were cloned in the invasive cryptic species Middle East-Asia Minor 1 (MEAM1) of the whitefly B. tabaci complex. Alignment of deduced amino acids sequences of both BtTres revealed that they share common consensus regions and residues with Tres of other insect species. Levels of BtTres expression in various stages and tissues of the whitefly suggested that BtTre-2 may play a key role in trehalose catabolism during development of the whitefly, especially for oocyte development, while BtTre-1 may prevent trehalose in salivary gland from leaking and entering into plants along with saliva. Potential roles of trehalose catabolism in response to direct and/or plant-mediated indirect effects of Tomato Yellow Leaf Curl China Virus (TYLCCNV) were also detected. Whiteflies feeding on virus-infected tobacco plants showed higher BtTres expressions and accordingly higher BtTres activity but lower trehalose content than those feeding on uninfected plants. The enhanced trehalose catabolism may be beneficial to oocyte development in ovary and attenuate plant defensive responses induced by trehalose in saliva. Viruliferous and nonviruliferous whiteflies feeding on cotton, a nonhost plant for TYLCCNV, differed significantly only in trehalose content. The higher trehalose content in viruliferous whiteflies may be conducive to resisting the stress inflicted by TYLCCNV.

show abstract

Trehalose and Abiotic Stress Tolerance

López‐Gómez

Lluch

2011

Abiotic Stress Responses in Plants

View full text Add to dashboard Cite

The Arabidopsis thaliana trehalase is a plasma membrane‐bound enzyme with extracellular activity

Cited by 49 publications

References 31 publications

Overexpression of the Trehalase Gene AtTRE1 Leads to Increased Drought Stress Tolerance in Arabidopsis and Is Involved in Abscisic Acid-Induced Stomatal Closure

Overexpression of the Trehalase Gene AtTRE1 Leads to Increased Drought Stress Tolerance in Arabidopsis and Is Involved in Abscisic Acid-Induced Stomatal Closure

MOLECULAR CHARACTERIZATION OF SOLUBLE AND MEMBRANE‐BOUND TREHALASES OF THE WHITEFLY, Bemisia tabaci

Trehalose and Abiotic Stress Tolerance

Contact Info

Product

Resources

About