Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon

Science

Volumn 274, Issue 5284, 1996, Pages 103-106

  Rep, Martijn ^a   Van Dijl, Jan Maarten ^b   Suda, Kitaru ^b   Schatz, Gottfried ^b   Grivell, Leslie A ^a   Suzuki, Carolyn K ^b  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b UNIVERSITY OF BASEL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; METALLOPROTEINASE; SERINE PROTEINASE;

ARTICLE; BINDING SITE; IMMUNOBLOTTING; MITOCHONDRIAL MEMBRANE; MITOCHONDRION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; YEAST;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ATP-DEPENDENT PROTEASES; BASE SEQUENCE; BINDING SITES; ELECTRON TRANSPORT COMPLEX IV; FUNGAL PROTEINS; HEAT-SHOCK PROTEINS; MEMBRANE PROTEINS; METALLOENDOPEPTIDASES; MITOCHONDRIA; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTON-TRANSLOCATING ATPASES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SERINE ENDOPEPTIDASES;

EID: 0029762950     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5284.103     Document Type: Article

References (38)

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34. 35S]methionine essentially as described [T. Langer, A. Pajic, I. Wagner, W. Neupert, Methods Enzymol. 260, 495 (1995)]. Labeling was terminated with 20 mM unlabeled methionine and 100 μM puromycin; the mitochondria were washed three times with 0.6 M mannitol, 2 mM EGTA, and 10 mM tris-maleate (pH 6.8), incubated at 37°C, and assayed for trichloroacetic acid (TCA)-precipitable radioactivity at the indicated times.
35. 35S]methionine essentially as described [T. Langer, A. Pajic, I. Wagner, W. Neupert, Methods Enzymol. 260, 495 (1995)]. Labeling was terminated with 20 mM unlabeled methionine and 100 μM puromycin; the mitochondria were washed three times with 0.6 M mannitol, 2 mM EGTA, and 10 mM tris-maleate (pH 6.8), incubated at 37°C, and assayed for trichloroacetic acid (TCA)-precipitable radioactivity at the indicated times.
36. 125I-labeled protein A and autoradiography.
37. 1 ATPase and to mitochondrial hsp60. For quantitation, different amounts of protein were loaded to ensure that measurements were within the linear range; these different samples were prepared from 800, 400, and 200 μg of mitochondrial protein.
38. Supported by grants from the Swiss National Science Foundation (to G.S.), the Human Capital and Mobility Program of the European Union (to G.S. and L.A.G.), EMBO (to M.R. and J.M.v.D.), and the Damon Runyon-Walter Winchell Cancer Research Foundation (to C.K.S.).