Purification of Saccharomcyes cerevisiae mitochondria devoid of microsomal and cytosolic contaminations

Analytical Biochemistry

Volumn 287, Issue 2, 2000, Pages 339-342

  Meisinger, Chris ^a   Sommer, Thomas ^b   Pfanner, Nikolaus ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY;

CEREVISIAE; CYTOSOLIC;

CHEMISTRY;

CHAPERONE; PROTEINASE K;

ARTICLE; CELL ORGANELLE; CONTAMINATION; CYTOSOL; MEDICAL RESEARCH; MICROSOME; MITOCHONDRION; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN TARGETING; PURIFICATION; SACCHAROMYCES CEREVISIAE; YEAST CELL;

SACCHAROMYCES CEREVISIAE;

EID: 0034672334     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.2000.4868     Document Type: Article

References (12)

1. Common principles of protein translocation across membranes
2. Protein import into mitochondria
3. Mitochondrial preprotein translocase
4. 2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
5. Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae
6. Successive translocation into and out of the mitochondrial matrix: Targeting of proteins to the intermembrane space by a bipartite signal peptide
7. Isolation of highly purified mitochondria from Saccharomyces cerevisiae
8. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
9. Evolutionary conservation of components of the protein translocation complex
10. Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors
11. Mitochondrial protein import: Nucleoside triphosphates are involved in conferring import-competence to precursors
12. The protein import motor of mitochondria: Unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70