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Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes : Two enzymes are present in potato mitochondria

Rasmusson, Allan G. LU ; Svensson, Å Staffan; Knoop, Volker; Grohmann, Lutz and Brennicke, Axel (1999) In Plant Journal 20(1). p.79-87
Abstract

Two different cDNAs, homologous to genes for rotenone-insensitive NADH dehydrogenases of bacteria and yeast, were isolated from potato. The encoded proteins, called NDA and NDB, have calculated molecular masses of 55 and 65kDa, respectively. The N-terminal parts show similarity to mitochondrial targeting peptides and the polypeptides are in vitro imported into potato mitochondria. Import processing to a smaller polypeptide is seen for the NDA but not the NDB protein. After import, NDA is intramitochondrially sorted to the matrix side of the inner membrane, whereas NDB becomes exposed to the intermembrane space. Imported proteins are associated to membranes upon digitonin permeabilization. On expression in Escherichia coli, NDB is... (More)

Two different cDNAs, homologous to genes for rotenone-insensitive NADH dehydrogenases of bacteria and yeast, were isolated from potato. The encoded proteins, called NDA and NDB, have calculated molecular masses of 55 and 65kDa, respectively. The N-terminal parts show similarity to mitochondrial targeting peptides and the polypeptides are in vitro imported into potato mitochondria. Import processing to a smaller polypeptide is seen for the NDA but not the NDB protein. After import, NDA is intramitochondrially sorted to the matrix side of the inner membrane, whereas NDB becomes exposed to the intermembrane space. Imported proteins are associated to membranes upon digitonin permeabilization. On expression in Escherichia coli, NDB is released from the bacterial membrane in the absence of divalent cations whereas detergents are necessary for solubilization of NDA. Both deduced amino-acid sequences contain the dual motifs for nucleotide binding with the characteristics of the core criteria, similar to the bacterial homologues. Unique among NADH dehydrogenases, the NDB amino-acid sequence contains a nonconserved insert, which is similar to EF-hand motifs for calcium binding. Phylogenetic analyses group the rotenone-insensitive NADH dehydrogenases largely by species, but suggest ancient gene duplications.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Plant Journal
volume
20
issue
1
pages
9 pages
publisher
Wiley-Blackwell
external identifiers
  • Scopus:0033213361
ISSN
0960-7412
DOI
10.1046/j.1365-313X.1999.00576.x
language
English
LU publication?
yes
id
6c833bbb-c3c8-4bcc-89d3-6c6c0044aa83
date added to LUP
2016-05-31 21:24:18
date last changed
2016-08-10 13:57:38
@misc{6c833bbb-c3c8-4bcc-89d3-6c6c0044aa83,
  abstract     = {<p>Two different cDNAs, homologous to genes for rotenone-insensitive NADH dehydrogenases of bacteria and yeast, were isolated from potato. The encoded proteins, called NDA and NDB, have calculated molecular masses of 55 and 65kDa, respectively. The N-terminal parts show similarity to mitochondrial targeting peptides and the polypeptides are in vitro imported into potato mitochondria. Import processing to a smaller polypeptide is seen for the NDA but not the NDB protein. After import, NDA is intramitochondrially sorted to the matrix side of the inner membrane, whereas NDB becomes exposed to the intermembrane space. Imported proteins are associated to membranes upon digitonin permeabilization. On expression in Escherichia coli, NDB is released from the bacterial membrane in the absence of divalent cations whereas detergents are necessary for solubilization of NDA. Both deduced amino-acid sequences contain the dual motifs for nucleotide binding with the characteristics of the core criteria, similar to the bacterial homologues. Unique among NADH dehydrogenases, the NDB amino-acid sequence contains a nonconserved insert, which is similar to EF-hand motifs for calcium binding. Phylogenetic analyses group the rotenone-insensitive NADH dehydrogenases largely by species, but suggest ancient gene duplications.</p>},
  author       = {Rasmusson, Allan G. and Svensson, Å Staffan and Knoop, Volker and Grohmann, Lutz and Brennicke, Axel},
  issn         = {0960-7412},
  language     = {eng},
  number       = {1},
  pages        = {79--87},
  publisher    = {ARRAY(0x9081b00)},
  series       = {Plant Journal},
  title        = {Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes : Two enzymes are present in potato mitochondria},
  url          = {http://dx.doi.org/10.1046/j.1365-313X.1999.00576.x},
  volume       = {20},
  year         = {1999},
}