Can a non-Mendelian mutation affect both chloroplast and mithchondrial ribosomes?

Abstract

Chloroplast ribosomes isolated from a spectinomycin-resistant mutant (spr-1-27-3) of Chlamydomonas reinhardtii that displays non-Mendelian inheritance fail to bind labeled antibiotic, in contrast to ribosomes from wild-type cells. In vitro resistance of this mutant appears to result from the absence of a specific protein in the small subunit of the chloroplast ribosome. However, chloroplast protein synthesis in the mutant and wild type shows identical sensitivity to spectinomycin in short-term in vivo experiments where ribulosediphosphate carboxylase serves as the marker. Long-term experiments demonstrate that the mutant can grow in the presence of spectinomycin only when acetate is supplied as a carbon source. Mitochondrial structure and function of the mutant are not affected by the antibiotic, whereas chloroplast structure and function are. Apparently, the mitochondrion, rather than the chloroplast, of this mutant is resistant to spectinomycin in vivo. We hypothesize that the gene product of the spr locus is a protein common to both chloroplast and mitochondrial ribosomes. The mutant gene product, in vivo, confers resistance on mitochondrial, but not chloroplast, ribosomes. We suppose that the mutant spr protein loosely attaches to chloroplast ribosomes in vivo so that the antibiotic is bound and blocks protein synthesis, but it dissociates during isolation, resulting in loss of the binding site.