TABLE 1.

Putative SlyA-regulated proteins of EIEC 12860 identified by MSa

Putative SlyA regulationSpotProteinGeneMol. mass (kDa)bpIb
Inductione1Chaperonin GroEL (chaperone Hsp60) mopA 57.144.85
2GroES (cochaperonin of GroEL) mopB 10.395.15
3DnaK (chaperone Hsp70) dnaK 68.984.83
4GrpE (cochaperone of DnaK) grpE 21.804.68
5Curved DNA-binding protein (CbpA) cbpA 34.466.33
6HdeA (periplasmic protein involved in acid resistance) hdeA 11.86/9.74d5.06/4.68
7HdeB (periplasmic protein involved in acid resistance) hdeB 12.04/9.075.73/4.94
8Glutamate decarboxylase alpha (GadA) gadA 52.695.22
9Hydrogenase 1, large subunit (HyaB) hyaB 66.255.61
10SAICAR synthetase (PurC) purC 26.995.07
11Aspartate transcarbamoylase, catalytic subunit (PyrB) pyrB 34.306.13
12GAPDH-C (GapC) gapC 35.755.45
13Transaldolase A (TalA) talA 35.665.89
14Periplasmic molybdate-binding protein (ModA) modA 27.36/24.927.81/6.38
15YbaS (putative glutaminase) ybaS 32.904.81
16Starvation lipoprotein (Slp; outer membrane protein) slp 20.96/19.096.82/6.32
17YhiU (putative membrane protein) yhiU 41.19/38.895.73/5.12
18YfiD (function unknown) yfiD 14.285.09
19YjgF (function unknown) yjgF 13.485.36
20Cytolysin A (ClyA, HlyE, SheA)c clyA 33.765.08
Repressionf21HisA (phosphoribosylformimino-5-amino-1-phosphoribosyl-4-imidazole carboxamide isomerase) hisA 26.034.94
22HisB (imidazoleglycerolphosphate dehydratase; histidinol phosphatase) hisB 40.285.76
23HisD (histidinol dehydrogenase) hisD 45.985.19
24HisF (cyclase) hisF 28.455.03
25HisG (ATP phosphoribosyltransferase) hisG 33.375.47
26Phenylalanyl-tRNA synthetase, α-subunit (PheS) pheS 36.835.79
27UPRTase upp 22.535.32
28Periplasmic ribose-binding protein (RbsB) rbsB 30.95/28.476.85/5.99
29RbsD (membrane-associated protein of the high-affinity ribose transporter) rbsD 16.706.36
30YkfE (function unknown) ykfE 16.87/14.106.27/5.51
31YnaF (function unknown) ynaF 16.025.60
32YcaC (function unknown) ycaC 23.105.20
33YfeU (function unknown) yfeU 31.225.70
  • a Whole-cell lysate proteins from bacteria grown to the stationary phase were analyzed.

  • b Theoretical molecular (mol.) masses and pI values of the E. coli proteins were calculated from the corresponding amino acid sequences deposited in the Swiss-Prot database by using ExPASy proteomics tool Compute pI/Mw (http://www.expasy.ch ).

  • c ClyA was detected only on the 2D protein map of EIEC 12860/pAL105, not on the maps of EIEC 12860 and EIEC 12860slyA.

  • d Value for the precursor protein/value for the processed protein (after removal of the signal peptide).

  • e Proteins show higher expression levels in EIEC 12860 and EIEC 12860/pAL105 than in EIEC 12860slyA.

  • f Proteins show higher expression levels in EIEC 12860slyA than in EIEC 12860 and EIEC 12860/pAL105.