ISSN:
1573-5028
Keywords:
Synechocystis sp. PCC6803
;
NAD(P)H-plastoquinone oxidoreductase
;
ndhA
;
ndhI
;
ndhG
;
ndhE
;
ndhE
;
ndhD
;
psaC
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The plastid DNA of higher plants contains eleven reading frames that are homologous to subunits of the mitochondrial NADH-ubiquinone oxidoreductase (complex I). The genes are expressed, but a plastid NAD(P)H dehydrogenase has not yet been isolated and the function of the enzyme in plastid metabolism is unknown. Cyanobacteria also contain a NADH dehydrogenase that is homologous to the mitochondrial complex I. The enzyme is sensitive to rotenone and is located on the cytoplasmic and the thylakoid membrane. We report here the sequence of five subunits (ndhA,-I, G,-E and -D) of the NADH dehydrogenase from the unicellular cyanobacterium Synechocystis sp. PCC6803. As in plastid DNA, the genes ndh(A-I-G-E) are clustered and probably constitute an operon. The ndhD gene is associated with a gene encoding an iron-sulphur protein of photosystem I (psaC) as in plastid DNA. In contrast to the situation in plastids, psaC and ndhD are not cotranscribed but transcribed from opposite strands. The deduced amino acid sequence of the cyanobacterial polypeptides is more similar to the corresponding plastid (40–68% identity) than to the corresponding mitochondrial subunits (17–39% identity). Thus, the cyanobacterial NADH-dehydrogenase provides a prokaryotic model system which is more suitable to genetic analysis than the enzyme of plastids.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00028896
Permalink
