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. 2006 Dec 8;189(3):844–850. doi: 10.1128/JB.01261-06

TABLE 2.

RPP cleaves mitochondrial presequence peptides

Peptidea Peptide sequence and sites of cleavage by RPP and MPPb Degradation by RPPc (%)
1 LSALARPVGAALRRSFSTSAQNNAKVA 59
2 MLAAKNILNRSSLSSSFRIATRLQSTKVQGSA 39
3 LSRVAKRAFSSTVANP 20
4 MLRAALTTVRRGPRLSRLLSAAATSAVPA 17
5 MFSKLAHLQRPAVLSRGVHSSVASA 17
6 MLSAARLQFAQGSVRRLTVSARDAPTKISTLA 9.5
7 GRWRLLVRPRAGAGGLRGSRGPGLGGGAVATRTLSV 7.3
8 LSLRQSIRFFKPATRTLCSSTYLL <1
a

Peptide 1, mouse MDH2-28; 2, yeast heat shock protein SSC1 (amino acids 1 to 32); 3, yeast MDH2-17; 4, mouse aldehyde dehydrogenase (amino acids 1 to 29); 5, human ornithine aminotransferase (amino acids 1 to 25); 6, yeast ubiquinol cytochrome c reductase subunit 2 (amino acids 1 to 32); 7, bovine ADX18-57; 8, yeast COXIV2-25.

b

Arrows (↓) denote RPP cleavage sites for peptides that can be detected or MPP cleavage sites (↑).

c

Cleavage efficiencies are determined as described in Materials and Methods.