Linked Life Data

7737352

Source:http://linkedlifedata.com/resource/pubmed/id/7737352

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-6-5
pubmed:abstractText
Tetrahymena 14-nm filament protein has been shown to have dual functions as a citrate synthase in mitochondria and as a cytoskeletal protein in oral morphogenesis and pronuclear behavior during conjugation. Immunofluorescence studies of the 14-nm filament protein/citrate synthase in mitochondria found that intense mitochondrial fluorescence remained unchanged in Tetrahymena cells taken from logarithmic growth phase to stationary phase. However, electron microscopic studies showed that electron-dense rod-shaped structures found in mitochondrial matrices tended to increase in Tetrahymena cells in the growth decline phase. The rods were composed of side-by-side straight filaments with diameters of approximately 14 to 16 nm. Serial sections revealed that in Tetrahymena cells in growth decline phase, one to four electron-dense rods existed in the matrices of every mitochondrion. Immunoelectron microscopy using an anti-14-nm filament antibody clearly showed that a filament bundle of the electron-dense rod was the bundle of polymerized filaments of 14-nm filament protein/citrate synthase. These results strongly suggest that dynamic monomer-polymer conversion of the 14-nm filament protein/citrate synthase in mitochondria depends upon the physiological conditions of Tetrahymena cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:volume
218
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
123-31
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Tetrahymena intramitochondrial filamentous inclusions contain 14-nm filament protein/citrate synthase.
pubmed:affiliation
Institute of Biological Sciences, University of Tsukuba, Ibaraki, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't