EMBO reports 3, 1099–1105, 2002
In the above paper, Table 2 was incorrectly printed. The rate constants for actomysin should be in bold type to distinguish them from those of myosin. The publisher would like to apologise for this error and any confusion caused. The correct version is printed below.
Table 2.
Transient kinetic analysis of actin with mutants and wild-type myosin
| Nucleotide | Rate constant | M761–2R | F506G-2R | F487A-2R |
|---|---|---|---|---|
| Nucleotide binding to actomyosin | ||||
| ATP | K1k+2 (M−1s−1) | 5.7 ± (0.4) × 105 | 4.8 ± (0.2) × 105 | 3.7 ± (0.2) × 105 |
| K1 (s−1) | 1000 | 500 | 400 | |
| k+2 (s−1) | ∼500 | >1000 | >1000 | |
| ADP | KAD (μM) | 182 ± (28) | 44 ± (6) | 84 ± (9) |
| k+AD (M−1s−1) | >0.5 × 106 | >0.5 × 106 | >0.2 × 106 | |
| k−AD (s−1) | >100 | >20 | >20 | |
| KAD/KD | 24 ± (3) | 28 ± (4) | 27 ± (3) | |
| Actin binding to myosin | ||||
| k+A (M−1s−1) | 8.0 ± (0.1) × 105 | 2.7 ± (0.3) × 105 | 8.0 ± (0.1) × 105 | |
| k−A (ms−1) | 2.5 ± (0.4) | 1.6 ± (0.3) | 5.0 ± (1) | |
| KA (nM) | 3.1 ± (0.5) | 5.9 ± (0.7) | 6.2 ± (0.8) | |
| KDA (nM) | 79.5 ± (14) | 162 ± (23) | 168 ± (29) | |
| k+DA (μM−1s−1) | 0.14 ± (0.01) | 0.11 ± (0.01) | 0.28 ± (0.02) | |
| k−DA (s−1) | 11.1 ± × 10−3 | 17.8 ± × 10−3 | 47.0 ± × 10−3 | |
| k−DA/k−A | 4.4 ± 0.6 | 11.1 ± 1.3 | 9.4 ± 0.8 | |
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Actomyosin interactions were analysed in terms of the schemes shown above (Millar and Geeves, 1983; Siemankowski and White, 1984).