Premium
cDNA‐derived amino acid sequence of rat mitochondrial 3‐oxoacyl‐CoA thiolase with no transient presequence: structural relationship with peroxisomal isozyme.
Author(s) -
Arakawa H.,
Takiguchi M.,
Amaya Y.,
Nagata S.,
Hayashi H.,
Mori M.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb02376.x
Subject(s) - thiolase , biology , peroxisome , peroxisomal targeting signal , complementary dna , biochemistry , mitochondrion , peptide sequence , amino acid , mitochondrial matrix , untranslated region , messenger rna , cytosol , gene , enzyme
The sorting of homologous proteins between two separate intracellular organelles is a major unsolved problem. 3‐Oxoacyl‐CoA thiolase is localized in mitochondria and peroxisomes, and provides a good system for the study on the problem. Unlike most mitochondrial matrix proteins, mitochondrial 3‐oxoacyl‐CoA thiolase in rats is synthesized with no transient presequence and possess information for mitochondrial targeting and import in the mature protein. Two overlapping cDNA clones contained an open reading frame encoding a polypeptide of 397 amino acid residues (predicted Mr = 41,868), a 5′ untranslated sequence of 164 bp, a 3′ untranslated sequence of 264 bp and a poly(A) tract. The amino acid sequence of the mitochondrial thiolase is 37% identical with that of the mature portion of rat peroxisomal 3‐oxoacyl‐CoA thiolase precursor. These results suggest that the two thiolases have a common origin and obtained information for targeting to respective organelles during evolution. Two portions in the mitochondrial thiolase that may serve as a mitochondrial targeting signal are presented.