Physiological, biochemical and molecular aspects of mitochondrial complex I in plants

Rasmusson, Allan G.; Heiser, Volker; Zabaleta, Eduardo; Brennicke, Axel; Grohmann, Lutz

doi:10.1016/s0005-2728(98)00021-8

Cited by 95 publications

(62 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Complex I in higher eukaryotes consists of more than 40 subunits. It pumps protons from the oxidation of matrix NADH across the mitochondrial inner membrane (Rasmusson et al, 1998). The 'activation' of Complex I in the mutant cells of sto1-during xylose metabolism implies that PsSto1p is part of the machinery that supports NADH oxidation.…”

Section: Expressing Pssto1 In S Cerevisiaementioning

confidence: 99%

“…These alternative components lie at the initial electron entry site (Site I) and the final quenching site (Site IV) of the ETC (Figure 1). Upstream of the ETC, rotenone-insensitive NAD(P)H dehydrogenases (non-proton-translocating) are present in addition to the rotenone-sensitive NADH dehydrogenase Complex I (proton-translocating) (Rasmusson et al, 1998). Downstream, an alternative terminal oxidase that is sensitive to salicylhydroxamic acid (SHAM) is present in addition to the standard cytochrome c oxidase (Cox) (Vanlerberghe and McIntosh, 1997).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

SHAM‐sensitive alternative respiration in the xylose‐metabolizing yeast Pichia stipitis

Shi

Cruz

Sherman

et al. 2002

Yeast

View full text Add to dashboard Cite

SHAM-sensitive (STO) alternative respiration is present in the xylose-metabolizing, Crabtree-negative yeast, Pichia stipitis, but its pathway components and physiological roles during xylose metabolism are poorly understood. We cloned PsSTO1, which encodes the SHAM-sensitive terminal oxidase (PsSto1p), by genome walking from wild-type CBS 6054 and subsequently deleted PsSTO1 by targeted gene disruption. The resulting sto1-deletion mutant, FPL-Shi31, did not contain other isoforms of Sto protein that were detectable by Western blot analysis using an alternative oxidase monoclonal antibody raised against the Sto protein from Sauromatum guttatum. Levels of cytochromes b, c, c 1 and a·a 3 did not change in the sto1-mutant, which indicated that deleting PsSto1p did not alter the cytochrome pool. Interestingly, the sto1-deletion mutant stopped growing earlier than the parent and produced 20% more ethanol from xylose. Heterologous expression of PsSTO1 in Saccharomyces cerevisiae increased its total oxygen consumption rate and imparted cyanide-resistant oxygen uptake but did not enable growth on ethanol, indicating that PsSto1p is not coupled to ATP synthesis. We present evidence that the mitochondrial NADH dehydrogenase complex (Complex I) was present in wild-type CBS 6054 but was bypassed in the cells during xylose metabolism. Unexpectedly, deleting PsSto1p led to the use of Complex I in the mutant cells when xylose was the carbon source. We propose that the non-proton-translocating NAD(P)H dehydrogenases are linked to PsSto1p in xylose-metabolizing cells and that this non-ATP-generating route serves a regulatory function in the complex redox network of P. stipitis. Published in

show abstract

Section: Expressing Pssto1 In S Cerevisiaementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

SHAM‐sensitive alternative respiration in the xylose‐metabolizing yeast Pichia stipitis

Shi

Cruz

Sherman

et al. 2002

Yeast

View full text Add to dashboard Cite

show abstract

“…Complex I, well studied in mammals has 43 subunits and is the largest of all the complexes, and the same complex in plants is also very large and similar to the mammalian enzyme (Rasmusson et al, 1998). Complex III receives electrons from ubiquinone and is reduced by either complex I or complex II.…”

Section: Discussionmentioning

confidence: 99%

“…In plants antisense suppression of complex I activity through repression of the 55 kDa subunit results in healthy plants. However the reduced respiratory ability is insufficient for normal pollen development (Rasmusson et al, 1998) pointing to the feasibility of complex I control of male fertility.…”

Section: Discussionmentioning

confidence: 99%

Sugarcane genes related to mitochondrial function

et al. 2001

View full text Add to dashboard Cite

Mitochondria function as metabolic powerhouses by generating energy through oxidative phosphorylation and have become the focus of renewed interest due to progress in understanding the subtleties of their biogenesis and the discovery of the important roles which these organelles play in senescence, cell death and the assembly of iron-sulfur (Fe/S) centers. Using proteins from the yeast Saccharomyces cerevisiae, Homo sapiens and Arabidopsis thaliana we searched the sugarcane expressed sequence tag (SUCEST) database for the presence of expressed sequence tags (ESTs) with similarity to nuclear genes related to mitochondrial functions. Starting with 869 protein sequences, we searched for sugarcane EST counterparts to these proteins using the basic local alignment search tool TBLASTN similarity searching program run against 260,781 sugarcane ESTs contained in 81,223 clusters. We were able to recover 367 clusters likely to represent sugarcane orthologues of the corresponding genes from S. cerevisiae, H. sapiens and A. thaliana with E-value ≤ 10 -10 . Gene products belonging to all functional categories related to mitochondrial functions were found and this allowed us to produce an overview of the nuclear genes required for sugarcane mitochondrial biogenesis and function as well as providing a starting point for detailed analysis of sugarcane gene structure and physiology.

show abstract

“…[3][4][5] CI contains more than 30 nuclear and mitochondrial-encoded proteins, and genome coordination is required for full activity. 6 At least 14 CI subunits are highly conserved in other eukaryotic and prokaryotic enzymes and a set of 9 proteins widely found in eukaryotic complexes. 3 This complex catalyzes the oxidation of NADH and the subsequent transfer of electrons to ubiquinone, coupled to proton transport across the inner mitochondrial membrane.…”

Section: Introductionmentioning

confidence: 99%

A simple method for the addition of rotenone in Arabidopsis thaliana leaves

Maliandi

Rius

Busi

et al. 2015

Plant Signaling & Behavior

View full text Add to dashboard Cite

A simple and reproducible method for the treatment of Arabidopsis thaliana leaves with rotenone is presented. Rosette leaves were incubated with rotenone and Triton X-100 for at least 15 h. Treated leaves showed increased expression of COX19 and BCS1a, 2 genes known to be induced in Arabidopsis cell cultures after rotenone treatment. Moreover, rotenone/Triton X-100 incubated leaves presented an inhibition of oxygen uptake. The simplicity of the procedure shows this methodology is useful for studying the effect of the addition of rotenone to a photosynthetic tissue in situ.

show abstract

Physiological, biochemical and molecular aspects of mitochondrial complex I in plants

Cited by 95 publications

References 60 publications

SHAM‐sensitive alternative respiration in the xylose‐metabolizing yeast Pichia stipitis

SHAM‐sensitive alternative respiration in the xylose‐metabolizing yeast Pichia stipitis

Sugarcane genes related to mitochondrial function

A simple method for the addition of rotenone in Arabidopsis thaliana leaves

Contact Info

Product

Resources

About