K. Schmidtbleek et al., THE 28.5-KDA IRON-SULFUR PROTEIN OF MITOCHONDRIAL COMPLEX-I IS ENCODED IN THE NUCLEUS IN PLANTS, MGG. Molecular & general genetics, 253(4), 1997, pp. 448-454
The intrinsic 28.5-kDa iron-sulfur protein of complex I in the mitocho
ndrial respiratory chain is encoded in the nucleus in animals and fung
i, but specified by a mitochondrial gene in trypanosomes. In plants, t
he homologous protein is now found to be encoded by a single-copy nucl
ear gene in Arabidopsis thaliana and by two nuclear genes in potato. T
he cysteine motifs involved in binding two iron-sulfur clusters are co
nserved in the plant protein sequences. The locations of the seven int
rons, with sizes between 60 and 1700 nucleotides, are identical in the
A. thaliana and the two potato genes, while their primary sequences d
iverse considerably. The A + T contents of the intron sequences range
between 61% and 73%, as is characteristic for dicot plants, but are in
some instances not higher than in the adjacent exons. Here, differenc
es in T content may instead serve to discriminate exons and introns. I
n potato, both genes are expressed, with the highest levels found in f
lowers. Sequence similarities between the homologous nuclear and mitoc
hondrial genes indicate that the nuclear forms in animals and plants o
riginate from the endosymbiont genome.