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J Biol Chem, Vol. 274, Issue 48, 33999-34004, November 26, 1999
,
From the Eight genes (atpI, atpB,
atpE1, atpE2,
atpE3, atpF, atpH, and
atpA) upstream of and contiguous with the previously
described genes atpG, atpD, and
atpC were cloned from chromosomal DNA of Acetobacterium woodii. Northern blot analysis revealed that
the eleven atp genes are transcribed as a polycistronic
message. The atp operon encodes the
Na+-F1F0-ATPase of A. woodii, as evident from a comparison of the biochemically derived
N termini of the subunits with the amino acid sequences deduced from
the DNA sequences. The molecular analysis revealed that all of the
F1F0-encoding genes from Escherichia coli have homologs in the
Na+-F1F0-ATPase operon from
A. woodii, despite the fact that only six subunits were
found in previous preparations of the enzyme from A. woodii. These results unequivocally prove that the
Na+-ATPase from A. woodii is an enzyme of the
F1F0 class. Most interestingly, the gene
encoding the proteolipid underwent quadruplication. Two gene copies
(atpE2 and atpE3)
encode identical 8-kDa proteolipids. Two additional gene copies were
fused to form the atpE1 gene. Heterologous
expression experiments as well as immunolabeling studies with native
membranes revealed that atpE1 encodes a
duplicated 18-kDa proteolipid. This is the first demonstration of
multiplication and fusion of proteolipid-encoding genes in
F1F0-ATPase operons. Furthermore,
AtpE1 is the first duplicated proteolipid ever found to be
encoded by an F1F0-ATPase operon.
Institut für Mikrobiologie und Genetik
der Georg-August-Universität, Grisebachstrasse 8, 37077 Göttingen, Germany and the § Lehrstuhl für
Mikrobiologie der Ludwig-Maximilians-Universität,
Maria-Ward-Strasse 1a, 80638 München, Germany
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