Publication Date:
1996-10-04
Description:
Afg3p and Rca1p are adenosine triphosphate (ATP)-dependent metalloproteases in yeast mitochondria. Cells lacking both proteins exhibit defects in respiration-dependent growth, degradation of mitochondrially synthesized proteins, and assembly of inner-membrane complexes. Defects in growth and protein assembly, but not in degradation, were suppressed by overproduction of yeast mitochondrial Lon, an ATP-dependent serine protease. Suppression by Lon was enhanced by inactivation of the proteolytic site and was prevented by mutation of the ATP-binding site. It is suggested that the mitochondrial proteases Lon, Afg3p, and Rca1p can also serve a chaperone-like function in the assembly of mitochondrial protein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rep, M -- van Dijl, J M -- Suda, K -- Schatz, G -- Grivell, L A -- Suzuki, C K -- New York, N.Y. -- Science. 1996 Oct 4;274(5284):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Cell Biology, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8810243" target="_blank"〉PubMed〈/a〉
Keywords:
ATP-Dependent Proteases
;
Adenosine Triphosphatases/metabolism
;
Adenosine Triphosphate/metabolism
;
Amino Acid Sequence
;
Base Sequence
;
Binding Sites
;
Electron Transport Complex IV/metabolism
;
Fungal Proteins/*metabolism
;
Heat-Shock Proteins/genetics/*metabolism
;
Membrane Proteins/*metabolism
;
*Metalloendopeptidases
;
Mitochondria/*metabolism
;
Mitochondrial Proteins
;
Molecular Sequence Data
;
Mutagenesis, Site-Directed
;
Proton-Translocating ATPases/metabolism
;
Saccharomyces cerevisiae/genetics/growth & development/*metabolism
;
*Saccharomyces cerevisiae Proteins
;
Serine Endopeptidases/genetics/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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