Abstract

The overall aim of this project is to identify the mechanism of mitochondrial assembly. Mitochondria are the main sources of ATP in eukaryotic cells, but they are also essential for many other biochemical processes.
The specific aim of this project to isolate and characterize yeast mutants in which mitochondrial assembly is defective. Two such mutants (mas 1 and mas 2) have already been isolated using a """"""""brute force"""""""" screen. Additional mutants will be sought by a variety of selection procedures. The genes affected in such mutants will be isolated by genetic complementation with genomic DNA banks from wild-type yeast. Availability of the genes should give information on the properties and the function of the proteins which participate in mitochondrial assembly.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
1R01GM037803-01
Application #
3293537
Study Section
Cellular Biology and Physiology Subcommittee 1 (CBY)
Project Start
1987-01-01
Project End
1989-12-31
Budget Start
1987-01-01
Budget End
1987-12-31
Support Year
1
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
University of Basel
Department
Type
DUNS #
484650064
City
Basel
State
Country
Switzerland
Zip Code
CH - 4051

  Publications

Leighton, J; Schatz, G (1995) An ABC transporter in the mitochondrial inner membrane is required for normal growth of yeast. EMBO J 14:188-95
Hahne, K; Haucke, V; Ramage, L et al. (1994) Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments. Cell 79:829-39
Rospert, S; Muller, S; Schatz, G et al. (1994) Fusion proteins containing the cytochrome b2 presequence are sorted to the mitochondrial intermembrane space independently of hsp60. J Biol Chem 269:17279-88
Glick, B S; Wachter, C; Reid, G A et al. (1993) Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP. Protein Sci 2:1901-17
Horst, M; Jeno, P; Kronidou, N G et al. (1993) Protein import into yeast mitochondria: the inner membrane import site protein ISP45 is the MPI1 gene product. EMBO J 12:3035-41
Hannavy, K; Rospert, S; Schatz, G (1993) Protein import into mitochondria: a paradigm for the translocation of polypeptides across membranes. Curr Opin Cell Biol 5:694-700
Ramage, L; Junne, T; Hahne, K et al. (1993) Functional cooperation of mitochondrial protein import receptors in yeast. EMBO J 12:4115-23
Rospert, S; Junne, T; Glick, B S et al. (1993) Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES. FEBS Lett 335:358-60
Hines, V; Schatz, G (1993) Precursor binding to yeast mitochondria. A general role for the outer membrane protein Mas70p. J Biol Chem 268:449-54
Beasley, E M; Muller, S; Schatz, G (1993) The signal that sorts yeast cytochrome b2 to the mitochondrial intermembrane space contains three distinct functional regions. EMBO J 12:2303-11

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