| pubmed-article:8573793 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8573793 | lifeskim:mentions | umls-concept:C0014181 | lld:lifeskim |
| pubmed-article:8573793 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
| pubmed-article:8573793 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:8573793 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:8573793 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:8573793 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:8573793 | lifeskim:mentions | umls-concept:C1511695 | lld:lifeskim |
| pubmed-article:8573793 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:8573793 | pubmed:dateCreated | 1996-3-12 | lld:pubmed |
| pubmed-article:8573793 | pubmed:abstractText | During early stages of meiosis I, yeast mitochondria fuse to form a single continuous thread. Thereafter, portions of the mitochondrial thread are equally distributed to daughter cells. Using time-lapse fluorescence microscopy and a membrane potential sensing dye, mitochondria are resolved as small particles at the cell periphery in pre-meiotic, living yeast. These organelles display low levels of movement. During meiosis I, we observed a threefold increase in mitochondrial motility. Mitochondrial movements were linear, occurred at a maximum velocity of 25 +/- 6.7 nm/s, and resulted in organelle collision and fusion to form elongated tubular structures. Mitochondria do not co-localize with microtubules. Destabilization of microtubules by nocodazole treatment has no significant effect on the rate and extent of thread formation. In contrast, yeast bearing temperature-sensitive mutations in the actin-encoding ACT1 gene (act1-3 and act1-133) exhibit abnormal mitochondrial aggregation, fragmentation, and enlargement as well as loss of mitochondrial motility. In act1-3 cells, mitochondrial defects and actin delocalization occur only at restrictive temperatures. The act1-133 mutation, which perturbs the myosin-binding site of actin without significantly affecting actin cytoskeletal structure in meiotic yeast, results in mitochondrial morphology and motility defects at restrictive and permissive temperatures. These studies support a role for the actin cytoskeleton in the control of mitochondrial position and movements in meiotic yeast. | lld:pubmed |
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| pubmed-article:8573793 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8573793 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8573793 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8573793 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8573793 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8573793 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8573793 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:8573793 | pubmed:author | pubmed-author:SmithM GMG | lld:pubmed |
| pubmed-article:8573793 | pubmed:author | pubmed-author:LowP FPF | lld:pubmed |
| pubmed-article:8573793 | pubmed:author | pubmed-author:O'SullivanHH | lld:pubmed |
| pubmed-article:8573793 | pubmed:author | pubmed-author:SimonV RVR | lld:pubmed |
| pubmed-article:8573793 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8573793 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:8573793 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8573793 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8573793 | pubmed:pagination | 1381-96 | lld:pubmed |
| pubmed-article:8573793 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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