Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-2-22
pubmed:abstractText
Trehalase is ubiquitous in higher plants. So far, indications concerning its function are scarce, although it has been implicated in the detoxification of exogenous trehalose. A putative trehalase gene, T19F6.15, has been identified in the genome sequencing effort in Arabidopsis. Here we show that this gene encodes a functional trehalase when its cDNA is expressed in yeast, and that it is expressed in various plant organs. Furthermore, we present results on the distribution and activity of trehalase in Arabidopsis and we describe how inhibition of trehalase by validamycin A affects the plants response to exogenous trehalose (alpha-D-glucopyranosyl-[1, 1]-alpha-D-glucopyranoside). Trehalase activity was highest in floral organs, particularly in the anthers (approximately 700 nkat g(-1) protein) and maturing siliques (approximately 250 nkat g(-1) protein) and much lower in leaves, stems, and roots (less than 50 nkat g(-1) protein). Inhibition of trehalase in vivo by validamycin A led to the accumulation of an endogenous substance that had all the properties of trehalose, and to a strong reduction in sucrose and starch contents in flowers, leaves, and stems. Thus, trehalose appears to be an endogenous substance in Arabidopsis, and trehalose and trehalase may play a role in regulating the carbohydrate allocation in plants.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-10806243, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-10982426, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-16664835, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-2507544, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-3583921, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-365019, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-4377836, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-5379538, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-8275864, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-8354408, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-8647289, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-9008394, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-9302019, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-942051, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-9558455, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-9628011, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-9681009, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-9681010, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-9744870, http://linkedlifedata.com/resource/pubmed/commentcorrection/11161063-9952444
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1086-93
pubmed:dateRevised
2010-9-14
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Trehalose and trehalase in Arabidopsis.
pubmed:affiliation
Botanisches Institut der Universität, Basel, Hebelstrasse 1, CH-4056 Basel, Switzerland. joachim.mueller@unibas.ch
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't