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首页> 外文期刊>Biochemistry >Phosphorylation of a single head of smooth muscle myosin activates the whole molecule
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Phosphorylation of a single head of smooth muscle myosin activates the whole molecule

机译：单头平滑肌肌球蛋白的磷酸化激活整个分子

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摘要

Regulatory light chain (RLC) phosphorylation activates smooth and non-muscle myosin H, but it has not been established if phosphorylation of one head turns on the whole molecule. Baculovirus expression and affinity chromatography were used to isolate heavy meromyosin (HMM) containing one phosphorylated and one dephosphorylated RLC (I-P HMM). Motility and steady-state ATPase assays indicated that I-P HMM is nearly as active as HMM with two phosphorylated heads (2-P HMM). singleturnover experiments further showed that- both the dephosphorylated and phosphorylated heads of I -P HMM can be activated by actin. Singly phosphorylated full-length myosin was also an active species with two cycling heads. Our results suggest that phosphorylation of one RLC abolishes the asymmetric inhibited state formed by dephosphorylated myosin [Liu, J., et al. (2003) J. Mol. Biol. 329, 963-972], allowing activation of both the phosphorylated and dephosphorylated heads. These findings help explain how smooth muscles are able to generate high levels of stress with low phosphorylation levels.
机译：调节性轻链（RLC）磷酸化可激活平滑肌和非肌肉型肌球蛋白H，但如果一个头的磷酸化打开整个分子，则尚无定论。杆状病毒表达和亲和色谱法用于分离含有一种磷酸化和一种去磷酸化的RLC（I-P HMM）的重肌球蛋白（HMM）。运动性和稳态ATPase分析表明，I-P HMM的活性几乎与带有两个磷酸化头（2-P HMM）的HMM一样。单周转实验进一步表明-I -P HMM的去磷酸化和磷酸化头部均可被肌动蛋白激活。单磷酸化的全长肌球蛋白也是具有两个循环头的活性物种。我们的结果表明，一个RLC的磷酸化消除了由去磷酸化的肌球蛋白形成的不对称抑制状态[Liu，J.，et al。 （2003）J.Mol。生物学329，963-972]，从而激活了磷酸化和去磷酸化的头部。这些发现有助于解释平滑肌如何以低磷酸化水平产生高水平的压力。

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