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Unless otherwise stated, the data in the following tables come from experiments carried out in vitro using soluble components (and receptors in membrane fractions) of the chemotaxis pathway of E. coli. The information on this page is organised as follows:
Further information is available:
| Symbol | Description | Molecular weight (kDa) |
|---|---|---|
| T | Taxis receptor | 58-60 |
| R | CheR | 33 |
| B | CheB | 37 |
| W | CheW | 18 |
| A | CheA | 71 |
| Y | CheY | 14 |
| Z | CheZ | 24 |
| M | FliM | 38 |
| a | aspartate | - |
| s | serine | - |
| m | methyl group | - |
| p | phosphoryl group | - |
| Reaction | Binding constant (µM) | Notes (reference) |
|---|---|---|
| TT + W <—> TTW | 13 ± 2 8 ± 1 |
Binding to EEEE-Tar QQQQ-Tar with a 2:3 stoichiometry (Asinas & Weis, 2006) |
| TT + AA <—> TTAA | 1.4 ± 0.1 | Binding to QQQQ-Tar with a ~1:20 stoichiometry (Asinas & Weis, 2006) |
| W + AA <—> WAA | ~0.01 | T. maritima (Park et al., 2004) |
| TT + AA <—> TTAA | 1-2 | Binding to Tsr with a 1:10 stoichiometry (Levit et al., 2002) |
| TT + W <—> TTW | 10 | Binding to Tsr with a 1:1 stoichiometry (Levit et al., 2002) |
| TT + W <—> TTW | 11.0 ± 0.5 | Tar receptor (Boukhvalova et al., 2002) |
| W + AA <—> WAA | 6.0 ± 0.2 | Boukhvalova et al. (2002) |
| TT + a <—> TTa | 0.9 ± 0.4 2.5 ± 1.2 |
Tar, reducing conditions Tar, oxidising conditions (Winston et al., 2005) |
| TT + s <—> TTs | 10 ± 2 | Tsr (Levit & Stock, 2002) |
| TT + s <—> TTs | 10 ± 4 | Tsr (Murphy et al., 2001) |
| TTWWAA + s <—> TTsWWAA | 10 ± 2 | EEEEE-Tsr (Levit & Stock, 2002) |
| TTWWAA + s <—> TTsWWAA | 14 ± 1 | QEQEE-Tsr (Levit & Stock, 2002) |
| TTWWAA + s <—> TTsWWAA | 19 ± 4 | QEmQEmEm-Tsr (Levit & Stock, 2002) |
| TTWWAA + a <—> TTaWWAA | 3.5 ± 0.5 | Using EEEE-Tar from FRET between CheY and CheZ in vivo (Sourjik & Berg, 2002a) |
| TTWWAA + a <—> TTaWWAA | 7.1 ± 1.7 | Using QEQE-Tar in a cheRcheB strain (see above) (Sourjik & Berg, 2002a) |
| TTWWAA + a <—> TTaWWAA | 2-5 | Binding of second aspartate to Tar dimer is at least 500-fold weaker (Björkman et al., 2001) |
| (T) + R <—> (T)R | 11 | Binding of pentapeptide NWETF (C-terminus of major receptors) (Yi & Weis, 2002) |
| (T) + B <—> (T)B | 150 | See above (Barnakov et al., 2002) |
| Y + M <—> YM | 1.7 ± 0.2 | T. maritima FliMNM (residues 1-249 of 334) (Park et al., 2006) |
| Y + M <—> YM | 120 | Binding with a 1:1 stoichiometry in isolated, intact switch complexes (Sagi et al., 2003) |
| Yp + M <—> YpM | 0.039 ± 0.005 | Using CheYp analogue CheY.BeF3 (see above) (Park et al., 2006) |
| Yp + M <—> YpM | 4 ± 1 | See above (Sagi et al., 2003) |
| Yp + M <—> YpM | 3.7 ± 0.4 | In vivo (Sourjik & Berg, 2002b) |
| Yp + ZZ <—> YpZZ | 0.0071 | Using CheYp analogue CheY.BeF3 (Silversmith et al., 2008) |
| Reaction | Rate constant | Notes (reference) |
|---|---|---|
| AA —> AAp | 0.11 s-1
| With 5 mM Mg2+ and 2 mM ATP (Wolanin et al., 2006) |
|
| AA —> AAp | 0.039 ± 0.004 s-1
| With 5 mM Mg2+ and 1 mM ATP (Zhao & Parkinson, 2006) |
|
| AA —> AAp | 0.048 ± 0.005 s-1
| With 10 mM Mg2+; KM for ATP is 0.38 ± 0.02 mM (Stewart, 2005) |
|
| AA —> AAp | 0.024 ± 0.005 s-1
| With 5 mM Mg2+ and 1 mM ATP (Jahreis et al., 2004) |
|
| AA —> AAp | 0.12 ± 0.01 s-1
| With 5 mM Mg2+ and 2 mM ATP (Kott et al., 2004) |
|
| AA —> AAp | 0.074 s-1
| With 5 mM Mg2+ and 4 mM ATP (Shrout et al., 2003) |
|
| AA —> AAp | 0.4 s-1
| With 5 mM Mg2+ and 2 mM ATP (Francis et al., 2002) |
|
| AA —> AAp | 0.106 ± 0.008 s-1
| With 5 mM Mg2+ and 2 mM ATP (Levit et al., 2002) |
|
| AA —> AAp | 0.050 ± 0.005 s-1
| With 10 mM Mg2+ and 1 mM ATP; KM for ATP is 0.3 ± 0.1 mM (Hirschman et al., 2001) |
|
| TTWWAA —> TTWWAAp | 10.3 s-1
| With 5 mM Mg2+ and 2 mM ATP; Tsr receptor (Wolanin et al., 2006) |
|
| TTWWAA —> TTWWAAp | 27 s-1
| With 5 mM Mg2+ and 4 mM ATP; Tar receptor (Shrout et al., 2003) |
|
| TTWWAA —> TTWWAAp | 41 s-1
| With 5 mM Mg2+ and 2 mM ATP; Tsr receptor (Francis et al., 2002) |
|
| TTWWAA —> TTWWAAp | 60 ± 14 s-1
| With 5 mM Mg2+ and 2 mM ATP; Tsr receptor (Levit et al., 2002) |
|
| TTWWAA —> TTWWAAp | 0.04:0.42:0.85:1.9:3.1 | With 5 mM Mg2+ and 0.1 mM ATP; mean activities with 0:1:2:3:4 Q residues on Salmonella Tar relative to activity of QEQE (Bornhorst & Falke, 2001) |
| TTWWAA —> TTWWAAp | 0.03:0.42:1.0:2.6 | Activities of EEEE:QEEE:QEQE:QQQQ (see above) (Bornhorst & Falke, 2000) |
| TTWWAA —> TTWWAAp | - | With 5 mM Mg2+ and 2 mM ATP; KM of Salmonella AA for ATP is 0.309 ± 0.004 mM, and for TTWWAA with QQQQ-LZ-Tar cytoplasmic fragment is 0.171 ± 0.009 mM (Levit et al., 1999) |
| Reaction | Rate constant | Notes (reference) |
|---|---|---|
| AAp + Y —> AA + Yp | ~108 M-1 s-1 | With 10 mM Mg2+; kcat/KM (Stewart et al., 2000) |
| AAp + B —> AA + Bp | 1.5 x 107 M-1 s-1 | See above (Stewart, personal communication) |
| Y —> Yp | 6 M-1 s-1 | With 20 mM Mg2+; kcat/KM for acetyl phosphate (Silversmith et al., 2001) |
| Y —> Yp | 8 M-1 s-1 | With 10 mM Mg2+; kcat/KM for acetyl phosphate (Schuster et al., 2001) |
| Y —> Yp | 3 M-1 s-1 | With 20 mM Mg2+; kcat/KM of Salmonella CheY for acetyl phosphate (Da Re et al., 1999) |
| Y —> Yp | 5 M-1 s-1 | With 10 mM Mg2+; kcat/KM for acetyl phosphate (Mayover et al., 1999) |
| Yp + ZZ —> Y + ZZ | 4.9 ± 0.1 s-1 | With 10 mM Mg2+ (Silversmith et al., 2008) |
| Yp + ZZ —> Y + ZZ | 2.2 ± 0.1 s-1 | From FRET between CheY and FliM in vivo in the wt strain (Sourjik & Berg, 2002b) |
| Yp —> Y | 0.045 s-1 | With 10 mM Mg2+ (Stewart & VanBruggen, 2004) |
| Yp —> Y | 0.051 s-1 | With 10 mM Mg2+ (Smith et al., 2003) |
| Yp —> Y | 0.085 ± 0.001 s-1 | From FRET between CheY and FliM in vivo in a cheZ strain (Sourjik & Berg, 2002b) |
| Yp —> Y | 0.036 ± 0.006 s-1 | With 20 mM Mg2+ (Silversmith et al., 2001) |
| Yp —> Y | 0.044 s-1 | With 20 mM Mg2+ (Schuster et al., 2001) |
| Yp —> Y | 0.053 s-1 | With 10 mM Mg2+ (Schuster et al., 2000) |
| Yp —> Y | 0.034 s-1 | With 10 mM Mg2+ (Mayover et al., 1999) |
| Yp —> Y | 0.030 ± 0.002 s-1 | With 20 mM Mg2+; Salmonella CheY (Da Re et al., 1999) |
| Yp —> Y | 0.049 s-1 | With 10 mM Mg2+ (Appleby & Bourret, 1998) |
| Reaction | Rate constant | Notes (reference) |
|---|---|---|
| TTm + B —> TT + B | - | With 10 mM Mg2+; KM for Tar is 2.9 ± 1.4 µM (Barnakov et al., 2002) |
| TTm + B —> TT + B | 0.0255 ± 0.0097 s-1 | With 25 mM Mg2+; KM for Salmonella Tar is 4.5 ± 1.5 µM (Anand & Stock, 2002) |
| TTm + B —> TT + B | 0.0017 s-1 | With 25 mM Mg2+ (Anand et al., 1998) |
| TTm + Bp —> TT + Bp | 0.187 ± 0.049 s-1 | With 10 mM Mg2+; using receptor-activated CheA as phosphodonor; KM for Tar is 2.75 ± 0.9 µM; measured rate constant is underestimate of true kcat (see below) (Barnakov et al., 2002) |
| TTm + Bp —> TT + Bp | 0.1480 ± 0.0039 s-1 | With 25 mM Mg2+; using phosphoramidate as phosphodonor; KM for Salmonella Tar is 7.0 ± 0.9 µM; only ~65% of CheB is phosphorylated under these conditions (Anand & Stock, 2002) |
| TTm + Bp —> TT + Bp | 0.0490 ± 0.0045 s-1 | With 25 mM Mg2+; using phosphoramidate as phosphodonor (Anand et al., 1998) |
| Cell volume (fl) | Notes (reference) |
|---|---|
| 1.4 | Sourjik & Berg (2002b) |
| 1.32 ± 0.30 | At 0.1 Osm; calculated from average amount of protein per cell (0.41 ± 0.03 pg), protein/dry weight ratio (0.68 ± 0.07), and volume of cytoplasmic water per mg dry weight (2.19 ± 0.11 fl) (Cayley et al., 2000) |
| 0.50 | RP437 strain (Scharf et al., 1998) |
| 0.42 | AW405 strain (Scharf et al., 1998) |
| Protein | Copy number | Concentration of monomer (µM)* | Notes (reference) |
|---|---|---|---|
| Receptors (total) Tsr + Tar Trg |
15000 ± 1700 14000 ± 1700 440 ± 70 |
18 ± 2 17 ± 2 0.52 ± 0.08 |
RP437 strain in rich medium; total includes an estimate for Tap + Aer (Li & Hazelbauer, 2004) |
| CheA (total) CheA (long) CheA (short) |
6700 ± 1100 4500 ± 940 2200 ± 520 |
7.9 ± 1.3 5.3 ± 1.1 2.6 ± 0.6 |
See above |
| CheW | 6700 ± 890 | 7.9 ± 1.0 | See above |
| CheY | 8200 ± 310 | 9.7 ± 0.4 | See above |
| CheZ | 3200 ± 90 | 3.8 ± 0.1 | See above |
| CheB | 240 ± 10 | 0.28 ± 0.01 | See above |
| CheR | 140 ± 10 | 0.16 ± 0.01 | See above |
*Concentrations are based on a cell volume of 1.4 fl. See Li & Hazelbauer (2004) for data for RP437 in minimal medium and for OW1 in both rich and minimal media.
| Protein | Copy number (strain) | Concentration of monomer (µM) | Notes (reference) |
|---|---|---|---|
| Receptor complex | - | - | Ratio of Salmonella Tar dimers to CheA dimers is 6.7 ± 1.7 (QEEE), 5.4 ± 1.1 (QEQE), and 5.3 ± 0.5 (QQQQ) (Bornhorst & Falke, 2003) |
| CheY | 17500 ± 1000 (RP437) | 49 ± 3 | Tethering and swimming assays suggest ~30% of CheY is phosphorylated (Alon et al., 1998) |
| CheY | 6850 ± 1300 (AW405) 2750 ± 275 (RP437) |
27 ± 5 9 ± 1 |
Scharf et al. (1998) |
| CheZ | 3050 ± 580 (AW405) 1170 ± 170 (RP437) |
12 ± 2 4 ± 1 |
CheY:CheZ ratio in both strains is about the same (2.3:1) (Scharf et al., 1998) |
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| Site developed and maintained by Matthew Levin. This page updated 24 September 2008. |