Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-10-12
pubmed:abstractText
We have studied the subcellular localization of the acid S-like ribonuclease (RNase) LX in tomato (Lycopersicon esculentum Mill.) cells using a combination of biochemical and immunological methods. It was found that the enzyme, unexpectedly excluded from highly purified vacuoles, accumulates in the endoplasmic reticulum. The evidence that RNase LX is a resident of the endoplasmic reticulum (ER) is supported by an independent approach showing that the C-terminal peptide HDEF of RNase LX acts as an alternative ER retention signal in plants. For functional testing, the cellular distribution of chimeric protein constructs based on a marker protein, Brazil nut (Bertholletia excelsa) 2S albumin, was analyzed immunochemically in transgenic tobacco (Nicotiana tabacum) plants. Here, we report that the peptide motif is necessary and sufficient to accumulate 2S albumin constructs of both vacuolar and extracellular final destinations in the ER. We have shown immunochemically that RNase LX is specifically expressed during endosperm mobilization and leaf and flower senescence. Using immunofluorescence, RNase LX protein was detected in immature tracheary elements, suggesting a function in xylem differentiation. These results support a physiological function of RNase LX in selective cell death processes that are also thought to involve programmed cell death. It is assumed that RNase LX accumulates in an ER-derived compartment and is released by membrane disruption into the cytoplasma of those cells that are intended to undergo autolysis. These processes are accompanied by degradation of cellular components supporting a metabolic recycling function of the intracellular RNase LX.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-10190580, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-10570215, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-11031240, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-1150746, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-1376250, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-16668816, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-1822990, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-2449095, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-3186459, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-7797553, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-7894013, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-8159174, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-8319673, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-8624403, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-8819310, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-8938406, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-9076996, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-9218460, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-9225461, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-9368420, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-9484484, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-9742958, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-9763713, http://linkedlifedata.com/resource/pubmed/commentcorrection/11598219-9880376
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
436-49
pubmed:dateRevised
2010-9-14
pubmed:meshHeading
pubmed-meshheading:11598219-Amino Acid Motifs, pubmed-meshheading:11598219-Apoptosis, pubmed-meshheading:11598219-Biological Transport, pubmed-meshheading:11598219-Cell Aging, pubmed-meshheading:11598219-Cell Differentiation, pubmed-meshheading:11598219-Cell Fractionation, pubmed-meshheading:11598219-Cells, Cultured, pubmed-meshheading:11598219-Endoplasmic Reticulum, pubmed-meshheading:11598219-Endoribonucleases, pubmed-meshheading:11598219-Gene Expression Regulation, Enzymologic, pubmed-meshheading:11598219-Gene Expression Regulation, Plant, pubmed-meshheading:11598219-Germination, pubmed-meshheading:11598219-Immunoblotting, pubmed-meshheading:11598219-Immunohistochemistry, pubmed-meshheading:11598219-Lycopersicon esculentum, pubmed-meshheading:11598219-Plant Proteins, pubmed-meshheading:11598219-Plant Structures, pubmed-meshheading:11598219-Plants, Genetically Modified, pubmed-meshheading:11598219-Protein Sorting Signals, pubmed-meshheading:11598219-Protoplasts, pubmed-meshheading:11598219-Recombinant Fusion Proteins, pubmed-meshheading:11598219-Ribonucleases
pubmed:year
2001
pubmed:articleTitle
Tomato ribonuclease LX with the functional endoplasmic reticulum retention motif HDEF is expressed during programmed cell death processes, including xylem differentiation, germination, and senescence.
pubmed:affiliation
Martin-Luther-Universität Halle-Wittenberg, Biozentrum, Weinbergweg 22, D-06120 Halle, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't