ANALYSIS OF ELEMENTS IN THE SUBSTRATE REQUIRED FOR PROCESSING BY MITOCHONDRIAL PROCESSING PEPTIDASE

Citation
T. Ogishima et al., ANALYSIS OF ELEMENTS IN THE SUBSTRATE REQUIRED FOR PROCESSING BY MITOCHONDRIAL PROCESSING PEPTIDASE, The Journal of biological chemistry, 270(51), 1995, pp. 30322-30326
Citations number
39
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
270
Issue
51
Year of publication
1995
Pages
30322 - 30326
Database
ISI
SICI code
0021-9258(1995)270:51<30322:AOEITS>2.0.ZU;2-I
Abstract
We have recently demonstrated that synthetic peptides modeled on the e xtension peptide of malate dehydrogenase can be a good substrate of mi tochondrial processing peptidase and that arginine residues present at positions -2 or -3 and distant from the cleavage point were important for recognition by the enzyme (Niidome, T., Kitada, S., Shimokata, K. , Ogishima, T., and Ito, A. (1994) J. Biol. Chem. 269, 24719-24722). W e further investigated the elements required for substrates of the pro tease, To analyze the reaction by a more rapid yet quantitative method , we have developed intramolecularly quenched fluorescent substrates, Using the fluorogenic substrates we demonstrated that at least one of the proline and glycine between the distal and proximal arginine resid ues was also important while other connecting sequences were dispensab le, In addition, the protease showed considerable preference for aroma tic and, to a lesser extent, hydrophobic amino acids in the P-1'-posit ion. These results together with the previous data suggest that the pr oximal and distal arginine residues, proline and/or glycine between th em, and P-1' amino acid could be critical determinants for the specifi c cleavage of the substrates by the protease.