Abstract:
:In the plant Nicotiana plumbaginifolia, manganese superoxide dismutase (MnSOD) is synthesized in the cytoplasm as a preprotein and is subsequently translocated to the mitochondrial matrix with corresponding cleavage of an NH2-terminal leader sequence. To determine whether the plant enzyme could replace the endogenous SOD activities of Escherichia coli and yeast, constructions have been made in appropriate vectors for expression of the preprotein and the mature MnSOD. These were introduced into SOD-deficient strains for complementation studies. In E. coli, both forms of the protein were shown to be active and able to complement SOD deficiency to different degrees. Expression of the preprotein in a yeast strain lacking a mitochondrial MnSOD resulted in a restoration of wild-type growth, only possible if the plant protein was being targeted to the mitochondria. Subsequent studies revealed that the protein was processed and that the leader sequence was cleaved at the identical position as recognized by the mitochondrial peptidase of plants. The components mediating mitochondrial import thus appear to be highly conserved between plants and yeast.
journal_name
Proc Natl Acad Sci U S Aauthors
Bowler C,Alliotte T,Van den Bulcke M,Bauw G,Vandekerckhove J,Van Montagu M,Inzé Ddoi
10.1073/pnas.86.9.3237subject
Has Abstractpub_date
1989-05-01 00:00:00pages
3237-41issue
9eissn
0027-8424issn
1091-6490journal_volume
86pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
pub_type: 杂志文章
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
pub_type: 杂志文章
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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