Abstract:
:We have previously identified a protein with Mr approximately 40,000 (p40) that binds with high specificity and affinity to the 5'-untranslated leaders of mitochondrial mRNAs in yeast. Here we show that this protein is abundant, comprising about 0.4% of total mitochondrial protein. p40 is present in a cytoplasmic (rho degree) petite mutant that lacks mitochondrial protein synthesis and is therefore nuclear encoded. p40 can be detected by immunological techniques in cell lysates of several different pet mutants, specifically disturbed in the translation of individual mitochondrial mRNAs. It is thus not one of the translation factors defined by any of these mutations. In the case of a pet111 mutant, which is specifically blocked in the translation of COX2 mRNA, extracts still display COX2 mRNA binding activity, indicating that p40 complex formation in vitro is not dependent on the presence of PET111.
journal_name
Biochimiejournal_title
Biochimieauthors
Dekker PJ,Papadopoulou B,Grivell LAdoi
10.1016/0300-9084(91)90182-zsubject
Has Abstractpub_date
1991-12-01 00:00:00pages
1487-92issue
12eissn
0300-9084issn
1638-6183pii
0300-9084(91)90182-Zjournal_volume
73pub_type
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