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. Author manuscript; available in PMC: 2010 Jul 15.
Published in final edited form as: Biochemistry. 1995 Aug 1;34(30):9722–9733. doi: 10.1021/bi00030a010

Table 3.

Effect of Engineered Cysteines and Disulfides on in Vitro Phosphorylation

relative phosphorylation ratec

receptor conditiona fraction SSb (−) aspartate
(/WT (+)Asp)
(+) aspartate
(/WT (+)Asp)
maximum activityd
(/WT (−) Asp)
aspartate
regulatione (/WT)
WT (−) na 50 ±5 1.0 ±0.2 1.0 1.0
red na 50 ± 5 1.0 ±0.2 1.0 1.0
ox (O2, I2) na 50 ± 5 1.0 ±0.2 1.0 1.0
Me na 50 ± 5 1.0 ±0.2 1.0 1.0
M75C red 38 ±2 0.6 ±0.1 0.8 1.3
ox (O2) 0.9 ± 0.1 25 ±4 0.8 ±0.1 0.5 0.7
A72C red 61 ± 1 1.0 ±0.5 1.2 1.2
ox (I2) 0.8 ± 0.1 82 ± 2 2.4 ±0.1 1.6 0.7
S68C red 70 ± 4 0.6 ± 0.2 1.4 2.3
ox (I2) 0.9 ± 0.1 11 ±2 0.5 ±0.1 0.2 0.4
I65C red 39 ± 5 0.8 ±0.5 0.8 1.0
ox (O2) 0.8 ± 0.1 12 ± 2 1.3 ±0.7 0.2 0.2
L61C red 34 ± 2 0.6 ±0.5 0.7 1.1
ox (O2) 0.6 ± 0.1 19 ± 1 0.7 ± 0.4 0.4 0.6
N36C red 76 ± 12 1.3 ±0.2 1.5 1.2
ox (O2) 0.9 ± 0.1 43 ± 2 1.3 ±0.1 0.9 0.7
L33C red 3 ± 1 0.7 ± 0.3 0.1 0.1
ox (O2) 1.0 ± 0.1 16 ± 1 2.8 ± 0.7 0.3 0.1
L29C red 37 ± 3 0.8 ±0.1 0.7 0.9
ox (O2) 0.9 ± 0.1 37 ± 9 0.9 ± 0.2 0.7 0.8
Q22C red 1 ± 0.5 0.3 ±0.1 0.02 0.04
ox (I2) 0.9 ± 0.1 1 ± 0.2 0.2 ±0.1 0.02 0.04
red (Me) 28 ± 3 2.8 ±0.3 0.6 0.2
ox (Me,I2) 1.0 ± 0.1 7 ± 1 1.0 ±0.1 0.1 0.1
F18C red 1 ± 0.2 0.3 ± 0.2 0.02 0.04
ox (I2) 0.9 ± 0.1 19 ± 1 0.7 ± 0.3 0.4 0.5
L11C red 137 ±5 1.9 ±0.1 2.7 1.4
ox (I2) 0.7 ± 0.1 2 ± 0.4 1.0 ±0.3 0.04 0.03
V8C red 65 ± 7 1.1 ±0.2 1.3 1.2
ox (O2) 0.8 ± 0.1 5 ± 2 0.9 ±0.1 0.1 0.1
V7C red 8± 2 0.3 ±0.1 0.2 0.5
ox (O2) 0.6 ± 0.1 1 ± 0.1 0.4 ±0.1 0.02 0.01
R4C red 24 ± 3 1.1 ±0.1 0.5 0.4
ox (O2) 0.7 ± 0.1 2 ± 0.5 1.0 ±0.1 0.04 0.02
no Tar (−) na 1.0 ± 0.2 1.0 ±0.2 0.02 0.0
a

Isolated membranes were treated as described in Materials and Methods: no treatment (−); reduction by dithiothreitol (red); oxidation (ox) by molecular iodine (I2) or oxygen (O2); methylation by CheR prior to reduction or oxidation (Me).

b

Fraction of receptor population linked by disulfide bonds after oxidation.

c

Rate of CheY phosphorylation by the reconstituted receptor–CheW–CheA ternary kinase complex in the absence or presence of ligand, relative to the rate observed for the aspartate-occupied wild-type complex subjected to the same chemical treatment (1.2 fmol of Pi-CheY s−1). All rates are normalized to the same receptor concentration (3µM dimer). In the presence of ligand, CheY phosphorylation was dominated by the free kinase, yielding the same rate observed in the absence of the receptor (no Tar).

d

Rate of CheY phosphorylation by the unliganded receptor–CheW–CheA ternary kinase complex, relative to corresponding rate observed for the unliganded wild-type complex subjected to the same chemical treatment (61 fmol of Pj-CheY s−1 for 3 µM receptor dimer).

e

Effect of aspartate on the rate of CheY phosphorylation by the receptor–CheW–CheA ternary kinase complex, relative to the effect of aspartate on the wild-type complex subjected to the same chemical treatment (50-fold downregulation upon aspartate addition). Calculated as the ratio {([rate (−) Asp]/[rate (+) Asp]) −1}/49, yielding a range between 0 and 1 for no aspartate regulation or wild-type regulation, respectively.