Abstract:
:The lack of trehalose accumulation in most plant species has been partly attributed to the presence of an active trehalase. Although trehalose synthesis enzymes are thought to be cytosolic, and previous studies have indicated that trehalase activity is extracellular, the exact location of the enzyme has not yet been established in plant cell. We present evidence that the yet uncharacterised full-length Arabidopsis trehalase is a plasma membrane-bound protein, probably anchored to the membrane through a predicted N-terminal membrane spanning domain. The full-length AtTRE1, when expressed in yeast can functionally substitute for the extracellularly active trehalase Ath1p, by sustaining the growth of an ath1 null mutant strain on trehalose and at pH 4.8. We further demonstrate that AtTRE1 expressed in yeast is plasma membrane-bound as in plant cell. In light of these findings, the regulation of plant cell endogenous trehalose by trehalase is discussed.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Frison M,Parrou JL,Guillaumot D,Masquelier D,François J,Chaumont F,Batoko Hdoi
10.1016/j.febslet.2007.07.036subject
Has Abstractpub_date
2007-08-21 00:00:00pages
4010-6issue
21eissn
0014-5793issn
1873-3468pii
S0014-5793(07)00807-1journal_volume
581pub_type
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