Translation in a wheat germ cell-free system of RNA from mitochondria of the normal and Texas male-sterile cytoplasms of maize (Zea mays L.)
RNA isolated from etiolated seedling shoot mitochondria of maize (Zea mays L.) with normal (N) or Texas male-sterile (T) cytoplasm stimulated the incorporation of (35S)-methionine into protein when added to a cell-free protein-synthesizing system from wheat germ. Discrete polypeptides with molecular...
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Published in | Current genetics Vol. 25; no. 1; p. 73 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
United States
1994
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Subjects | |
Online Access | Get more information |
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Summary: | RNA isolated from etiolated seedling shoot mitochondria of maize (Zea mays L.) with normal (N) or Texas male-sterile (T) cytoplasm stimulated the incorporation of (35S)-methionine into protein when added to a cell-free protein-synthesizing system from wheat germ. Discrete polypeptides with molecular masses of up to approximately 67 kDa were synthesized, and the pattern of bands was distinct from that obtained with total RNA. Products of translation of T-urf13 RNA were identified by immunoprecipitation, and of atpA, cox1, and cox2 RNA by hybrid arrest of translation by the cloned gene. Several polypeptides were differentially synthesized from N and T mitochondrial RNA; these differences were more extensive than those found when isolated, intact, N and T mitochondria are allowed to synthesize proteins. |
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Bibliography: | 94B0042 F30 |
ISSN: | 0172-8083 1432-0983 |
DOI: | 10.1007/BF00712971 |