TABLE 2.

Novel proteolytic sites identified in mitochondrial proteins during EPEC infection^a

Gene	Protein name	N-terminal siteb	Fold change, WT:mock		Fold change, WT:ΔescN		T3S dependent?
			C	M	C	M
ACAA2	3-Ketoacyl-CoA thiolase, mitochondrial	KHKISR↓E177*		↑1.5
HSPD1	60-kDa heat shock protein, mitochondrial	ALNATR↓A430*	ns	ns	ns	↑1.6	Yes
ATP5A1	ATP synthase subunit alpha, mitochondrial	SILEER↓I59*		ns		↑1.7
CPS1	Carbamoyl-phosphate synthase [ammonia], mitochondrial	YPVMIR↓S588*		↑16.7
CPS1	Carbamoyl-phosphate synthase [ammonia], mitochondrial	FLVKGN↓D1250*		↑2.3
DUT	Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial	MPC↓S4*	↓1.7	↓2.9	ns	ns
NDUFAF3	NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 3	WAPRRG↓H32*	↑1.9	ns	ns	ns
HSPA9	Stress-70 protein, mitochondrial	NAEGAR↓T86*		ns		↑2.2	Yes
VDAC1	Voltage-dependent anion-selective channel protein 1	TDNTLG↓T83*	↑10.1	↑3.4	↓1.7	↓1.7	Yes

^aMitochondrial N-terminal peptides that were altered in abundance during EPEC infection are listed according to the N-terminal type, site, and relative fold change between EPEC wild-type (WT) infection versus either mock-infected cells or T3S-deficient infection (ΔescN). These sites have not been previously reported in the DegraBase or MS-TAILS experiments of apoptosis (16, 22). C, whole-cell fraction; M, mitochondrial fraction; bold text, protein known to be associated with apoptosis from UniProt; ↓, N-terminal location of observed N terminus in the full-length protein; ns, not significantly altered in abundance; *, previously unreported site in the DegraBase or MS-TAILS of apoptosis (16, 22).

^bN-terminal site denotes the six amino acids to the prime and nonprime sides of the predicted site of proteolysis (i.e., P6 to P6’).