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Circadian rhythms in Neurospora crassa: the effects of point mutations on the proteolipid portion of the mitochondrial ATP synthetase
Authors:Stuart Brody   Carol Dieckmann  Steve Mikolajczyk
Affiliation:(1) Department of Biology, University of California, San Diego, 92093 La Jolla, CA, USA;(2) Present address: Department of Biochemistry, University of Arizona, Tucson, AZ, USA
Abstract:Summary Five oligomycin-resistant (olir) mutant strains of Neurospora crassa were analyzed for their growth rate and for the periodicity of their circadian rhythm. The most resistant strains had periods of 18–19 h while the least resistant strain had a normal period of 21.0 h. There was a rough correlation between the in vivo degree of oligomycinresistance and the amount of change in the period. Several of the olir mutations have been previously described by Sebald et al. (1977) in terms of known amino acid changes in the primary structure of the proteolipid, or DCCD-binding protein, found in the F0 membrane portion of the mitochondrial ATP synthetase. Amino acid changes in the structure of this protein are reported here for two other olir mutations. The proteolipid isolation procedures were slightly modified to include a delipidation step, and an HPLC procedure was developed to separate the hydrophobic peptides of this protein. Analysis of heterocaryons carrying both the olir and olis markers indicated that the olir and olis mutations were codominant to each other in terms of period and growth rate. The changes in the primary structure of this DCCD-binding protein reported here are the first known examples of changes in the primary structure of a protein which alter the period of a circadian rhythm.
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