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Synthesis of a larger precursor for the proteolipid subunit of the mitochondrial ATPase complex of Neurospora crassa in a cell‐free wheat germ system
Author(s) -
Michel R.,
Wachter E.,
Sebald W.
Publication year - 1979
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(79)81047-9
Subject(s) - neurospora crassa , crassa , philosophy , chemistry , physics , humanities , art history , crystallography , polymer science , stereochemistry , art , biochemistry , mutant , gene
The proteolipid subunit of the ATPase complex from Neurospora CYQSSQ [l] is synthesized on cytoplasmic ribosomes [2] and coded for by a nuclear gene [3]. This raises the question of how this extremely hydrophobic protein [4] is transported into the mitochondria and how it is assembled with the numerous other subunit polypeptides to form the functional ATPase complex located in the mitochondrial inner membrane. Translation of polyadenylated RNA from Neurospora crussa in a cell-free system of wheat germ resulted in the synthesis of a polypeptide with an app. mol. wt -,12 000 that was specifically immunoprecipitated by antibodies raised against the authentic 8000 mol. wt proteolipid. The in vitro synthesis of a higher molecular weight precursor of the ATPase subunit is reminiscent of the preforms identified after in vitro synthes% of hormones and other secretory proteins (see e.g., [5]). We propose that the additional amino acid sequence plays a role either during the transfer of the proteolipid into the mitochondrion or during the assembly of the mitochondrial ATPase complex.