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Difference between revisions of "McDonald 2009 FEBS Lett"

From Bioblast
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{{Publication
{{Publication
|title=McDonald BM, Wydrob MM, Lightowlersb RN, Lakey JH (2009) Probing the orientation of yeast VDAC1 ''in vivo''. FEBS Lett 583: 739-742.
|title=McDonald BM, Wydrob MM, Lightowlers RN, Lakey JH (2009) Probing the orientation of yeast VDAC1 ''in vivo''. FEBS Lett 583: 739-742.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19185576 PMID: 19185576]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19185576 PMID: 19185576]
|authors=McDonald BM, Wydrob MM, Lightowlersb RN, Lakey JH
|authors=McDonald BM, Wydrob MM, Lightowlers RN, Lakey JH
|year=2009
|year=2009
|journal=FEBS Lett
|journal=FEBS Lett
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}}
}}
{{Labeling
{{Labeling
|area=Respiration, Genetic knockout;overexpression
|organism=Saccharomyces cerevisiae
|organism=Saccharomyces cerevisiae
|taxonomic group=Fungi
|taxonomic group=Fungi
|preparations=Intact cells
|preparations=Intact cells
|enzymes=Inner mtMembrane Transporter
|enzymes=Inner mtMembrane Transporter
|injuries=Genetic Defect; Knockdown; Overexpression
|couplingstates=OXPHOS
|instruments=Oxygraph-2k
|instruments=Oxygraph-2k
|discipline=Mitochondrial Physiology
|discipline=Mitochondrial Physiology
}}
}}

Revision as of 10:34, 12 August 2013

Publications in the MiPMap
McDonald BM, Wydrob MM, Lightowlers RN, Lakey JH (2009) Probing the orientation of yeast VDAC1 in vivo. FEBS Lett 583: 739-742.

Β» PMID: 19185576

McDonald BM, Wydrob MM, Lightowlers RN, Lakey JH (2009) FEBS Lett

Abstract: Voltage dependent anion channel (VDAC) is a vital ion channel in mitochondrial outer membranes and its structure was recently shown to be a 19 stranded beta-barrel. However the orientation of VDAC in the membrane remains unclear. We probe here the topology and membrane orientation of yeast Saccharomyces cerevisiae in vivo. Five FLAG-epitopes were independently inserted into scVDAC1 and their surface exposure in intact and disrupted mitochondria detected by immunoprecipitation. Functionality was confirmed by measurements of respiration. Two epitopes suggest that VDAC (scVDAC) has its C-terminus exposed to the cytoplasm whilst two others are more equivocal and, when combined with published data, suggest a dynamic behavior. β€’ Keywords: Mitochondrial membrane channels


Labels: MiParea: Respiration, Genetic knockout;overexpression 


Organism: Saccharomyces cerevisiae 

Preparation: Intact cells  Enzyme: Inner mtMembrane Transporter"Inner mtMembrane Transporter" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property. 


HRR: Oxygraph-2k