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. 2009 Sep 1;20(17):3941–3952. doi: 10.1091/mbc.E09-04-0346

Table 3.

In vitro activity of wild type and mutant forms of Myo2p

Myo2p samplea Activity (± SD)
In vitro motility (μm · s−1)b
    Wild type 0.42 ± 0.06
    Rlc1p-S35A-S36A 0.12 ± 0.04
    Rlc1p-S35D-S36D 0.41 ± 0.07
    Rlc1p-NΔ 0.46 ± 0.04
    Myo2p-S1444A 0.40 ± 0.06
    Myo2p-S1444D 0.44 ± 0.08
    Myo2p-S1444A/Rlc1p-S35A-S36A 0.14 ± 0.02
    Myo2p-S1444A/Rlc1p-S35D-S36D 0.46 ± 0.11
    Myo2p-S1444D/Rlc1p-S35A-S36A 0.16 ± 0.03
    Myo2p-S1444D/Rlc1p-S35D-S36D 0.59 ± 0.05
Actin-activated Mg2+-ATPasec
KM (μM) Vmax (s−1)d
Wild type 19.9 ± 3.2 3.2 ± 0.2
Rlc1p-S35A-S36A 16.9 ± 4.2 2.7 ± 0.2
Rlc1p-S35D-S36D 18.6 ± 4.3 3.0 ± 0.2

a Each Myo2p sample is made up of the Myo2p heavy chain, ELC Cdc4p, and Rlc1p. Relevant mutations are indicated.

b n = 60 filaments. Motility was performed using one-step purified Myo2p samples.

c ATPase values for Rlc1p-AA and -DD samples are derived from the curves in Figure 6A.

d ATPase activity: moles of ATP hydrolyzed per motor per second.