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Electrophoretic pattern of and amino acid incorporation in vitro into the insoluble mitochondrial protein of neurospora crassa wild type and mi‐1 mutant
Author(s) -
Sebald W.,
Bücher Th.,
Olbrich B.,
Kaudewitz F.
Publication year - 1968
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(68)80071-7
Subject(s) - neurospora crassa , mutant , microbiology and biotechnology , crassa , physics , crystallography , biology , humanities , chemistry , stereochemistry , philosophy , genetics , gene
The maternally inherited (mi) mutants of Neurospom craw exhibit polyphenic deviation in mitochondrial composition and function [ 1 ] . For instance in the first days of mycelial growth, the concentrations of cytochrome a and b are drastically reduced and those of cytochrome c and levels of fatty acids increased in the mutant compared to the wild type [2,3]. In this stage respiration is virtually cyanide insensitive [4]. These effects may originate from alterations of the amino acid sequence of ‘structural protein’, which is regarded as important in the organisation of the electron transport chain [5]. The mitochondrial DNA was thought to contain information for the amino acid sequence for structural protein and the mitochondrial deviations would originate from point mutations. However prep arations of ‘structural protein’ have been resolved electrophoretically into several fractions [6,7] and the experimental basis of the explanation of Woodward et al. is open to criticism. Recently techniques for the electrophoretic fractionation of complex insoluble mitochondrial proteins after incorporation of labelled amino acids in vitro have been developed [6,8]. In the experiments described here these techniques have been applied to the insoluble protein fraction of mitochondria (IMP) from the wild type and from m&l.