The role of Tim9p in the assembly of the TIM22 import complexes.
作者： Danielle Leuenberger , Sean P. Curran , David Wong , Carla M. Koehler
DOI: 10.1034/J.1600-0854.2003.00095.X
关键词:
摘要: Tim9p is located in the soluble 70-kDa Tim9p–Tim10p complex and 300-kDa membrane mitochondrial TIM22 protein import system, which mediates of inner proteins. From a collection temperature-sensitive mutants, we have analyzed two detail. tim9–3 contained mutations tim9–19 one mutation, all near ‘twin CX3C’ motif that conserved small Tim As result, components mutant mitochondria were severely reduced assembled into complexes aberrant sizes. Protein was Tim10p binding to vitro imported ADP/ATP carrier impaired. In mitochondria, assembled, although not detectable. decreased only two-fold. When coexpressed Escherichia coli, TIM10 proteins failed assemble complex. Our findings suggest residues are important for assembly both
sci-hub.se 参考文章(44)
S Rospert, G Schatz, B S Glick, S Müller, Fusion proteins containing the cytochrome b2 presequence are sorted to the mitochondrial intermembrane space independently of hsp60. Journal of Biological Chemistry. ,vol. 269, pp. 17279- 17288 ,(1994) , 10.1016/S0021-9258(17)32552-8
Michael P. Yaffe, Isolation and analysis of mitochondrial inheritance mutants from Saccharomyces cerevisiae. Methods in Enzymology. ,vol. 260, pp. 447- 453 ,(1995) , 10.1016/0076-6879(95)60157-0
Benjamin S. Glick, Liza A. Pon, Isolation of highly purified mitochondria from Saccharomyces cerevisiae. Methods in Enzymology. ,vol. 260, pp. 213- 223 ,(1995) , 10.1016/0076-6879(95)60139-2
Christian Sirrenberg, Maxi Endres, Heike Fölsch, Rosemary A. Stuart, Walter Neupert, Michael Brunner, Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5 Nature. ,vol. 391, pp. 912- 915 ,(1998) , 10.1038/36136
N Pfanner, P Hoeben, M Tropschug, W Neupert, The carboxyl-terminal two-thirds of the ADP/ATP carrier polypeptide contains sufficient information to direct translocation into mitochondria. Journal of Biological Chemistry. ,vol. 262, pp. 14851- 14854 ,(1987) , 10.1016/S0021-9258(18)48101-X
C L Dieckmann, R R Staples, Generation of Temperature-Sensitive Cbp1 Strains of Saccharomyces Cerevisiae by Pcr Mutagenesis and in Vivo Recombination: Characteristics of the Mutant Strains Imply That Cbp1 Is Involved in Stabilization and Processing of Cytochrome B Pre-mRNA Genetics. ,vol. 135, pp. 981- 991 ,(1993) , 10.1093/GENETICS/135.4.981
H. Schagger, W.A. Cramer, G. Vonjagow, Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Analytical Biochemistry. ,vol. 217, pp. 220- 230 ,(1994) , 10.1006/ABIO.1994.1112
E. Jarosch, G. Rödel, R. J. Schweyen, A soluble 12-kDa protein of the mitochondrial intermembrane space, Mrs11p, is essential for mitochondrial biogenesis and viability of yeast cells. Molecular Genetics and Genomics. ,vol. 255, pp. 157- 165 ,(1997) , 10.1007/S004380050484
Jürgen Bereiter-Hahn, Dimethylaminostyrylmethylpyridiniumiodine (DASPMI) as a fluorescent probe for mitochondria in situ Biochimica et Biophysica Acta. ,vol. 423, pp. 1- 14 ,(1976) , 10.1016/0005-2728(76)90096-7
Hermann Schägger, Gebhard von Jagow, Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Analytical Biochemistry. ,vol. 166, pp. 368- 379 ,(1987) , 10.1016/0003-2697(87)90587-2