CONVERSION OF A NONPROCESSED MITOCHONDRIAL PRECURSOR PROTEIN INTO ONE THAT IS PROCESSED BY THE MITOCHONDRIAL PROCESSING PEPTIDASE

被引:43
作者
WALTNER, M [1 ]
WEINER, H [1 ]
机构
[1] PURDUE UNIV,DEPT BIOCHEM,W LAFAYETTE,IN 47907
关键词
D O I
10.1074/jbc.270.44.26311
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mitochondrial processing peptidase (MPP) cleaves the signal sequence from a variety of mitochondrial pre cursor proteins. A subset of mitochondrial proteins, including rhodanese and 3-oxoacyl-CoA thiolase, are imported into the matrix space, yet are not processed. Rhodanese signal peptide and translated protein were recognized by MPP, as both were inhibitors of processing. The signal peptide of precursor aldehyde dehydrogenase consists of a helix-linker helix motif but when the RGP linker is removed, processing no longer occurs (Thornton, K., Wang, Y., Weiner, H., and Gorenstein, D. G. (1993) J. Biol. Chem. 268, 19906-19914). Disruption of the helical signal sequence of rhodanese by the addition of the RGP linker did not allow cleavage to occur. However, addition of a putative cleavage site allowed the protein to be processed. The same cleavage site was added to 3-oxoacyl-CoA thiolase, but this protein was still not processed, Thiolase and linker-deleted aldehyde dehydrogenase signal peptides were poor inhibitors of MPP. It can be concluded that both a processing site and the structure surrounding this site are important for MPP recognition.
引用
收藏
页码:26311 / 26317
页数:7
相关论文
共 42 条
[1]   THE NH2-TERMINAL 14-16 AMINO-ACIDS OF MITOCHONDRIAL AND BACTERIAL THIOLASES CAN DIRECT MATURE ORNITHINE CARBAMOYLTRANSFERASE INTO MITOCHONDRIA [J].
ARAKAWA, H ;
AMAYA, Y ;
MORI, M .
JOURNAL OF BIOCHEMISTRY, 1990, 107 (01) :160-164
[2]   CDNA-DERIVED AMINO-ACID-SEQUENCE OF RAT MITOCHONDRIAL 3-OXOACYL-COA THIOLASE WITH NO TRANSIENT PRESEQUENCE - STRUCTURAL RELATIONSHIP WITH PEROXISOMAL ISOZYME [J].
ARAKAWA, H ;
TAKIGUCHI, M ;
AMAYA, Y ;
NAGATA, S ;
HAYASHI, H ;
MORI, M .
EMBO JOURNAL, 1987, 6 (05) :1361-1366
[3]  
ARRETZ M, 1994, J BIOL CHEM, V269, P4959
[4]   BIOGENESIS OF MITOCHONDRIA [J].
ATTARDI, G ;
SCHATZ, G .
ANNUAL REVIEW OF CELL BIOLOGY, 1988, 4 :289-333
[5]  
BELTZER JP, 1988, J BIOL CHEM, V263, P368
[6]   CONFORMATIONAL-ANALYSIS OF A MITOCHONDRIAL PRESEQUENCE DERIVED FROM THE F1-ATPASE BETA-SUBUNIT BY CD AND NMR-SPECTROSCOPY [J].
BRUCH, MD ;
HOYT, DW .
BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1159 (01) :81-93
[7]   N-TERMINAL HALF OF A MITOCHONDRIAL PRESEQUENCE PEPTIDE TAKES A HELICAL CONFORMATION WHEN BOUND TO DODECYLPHOSPHOCHOLINE MICELLES - A PROTON NUCLEAR MAGNETIC-RESONANCE STUDY [J].
ENDO, T ;
SHIMADA, I ;
ROISE, D ;
INAGAKI, F .
JOURNAL OF BIOCHEMISTRY, 1989, 106 (03) :396-400
[8]  
FINOCCHIARO G, 1993, EUR J BIOCHEM, V213, P1103
[9]   CLEAVAGE-SITE MOTIFS IN MITOCHONDRIAL TARGETING PEPTIDES [J].
GAVEL, Y ;
VONHEIJNE, G .
PROTEIN ENGINEERING, 1990, 4 (01) :33-37
[10]   BIFUNCTIONAL ROLE OF THE BC(1) COMPLEX IN PLANTS - MITOCHONDRIAL BC(1) COMPLEX CATALYSES BOTH ELECTRON TRANSPORT AND PROTEIN PROCESSING [J].
GLASER, E ;
ERIKSSON, A ;
SJOLING, S .
FEBS LETTERS, 1994, 346 (01) :83-87