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棘阿米巴肌球蛋白II的酶活性和丝状体组装受尾部末端相邻结构域的调节。

Enzymatic activity and filament assembly of Acanthamoeba myosin II are regulated by adjacent domains at the end of the tail.

作者信息

Atkinson M A, Appella E, Corigliano-Murphy M A, Korn E D

机构信息

Laboratory of Cell Biology, National Heart, Lung and Blood Institute, Bethesda, MD 20892.

出版信息

FEBS Lett. 1988 Jul 18;234(2):435-8. doi: 10.1016/0014-5793(88)80132-7.

DOI:10.1016/0014-5793(88)80132-7
PMID:2968922
Abstract

Polyclonal antibodies raised against a synthetic peptide consisting of the last 19 amino acids at the end of the coiled-coil region of the heavy chains inhibited the actin-activated Mg2+-ATPase activity of myosin II and its ability to form filaments. Antibodies against a synthetic peptide corresponding to the 21 adjacent amino acids at the beginning of the non-helical tailpiece, which include the three regulatory phosphorylatable serines, had no effect on either activity.

摘要

针对由重链卷曲螺旋区域末端的最后19个氨基酸组成的合成肽产生的多克隆抗体,抑制了肌球蛋白II的肌动蛋白激活的Mg2 + -ATP酶活性及其形成细丝的能力。针对对应于非螺旋尾段起始处21个相邻氨基酸(包括三个可调节磷酸化的丝氨酸)的合成肽的抗体,对这两种活性均无影响。

相似文献

1
Enzymatic activity and filament assembly of Acanthamoeba myosin II are regulated by adjacent domains at the end of the tail.棘阿米巴肌球蛋白II的酶活性和丝状体组装受尾部末端相邻结构域的调节。
FEBS Lett. 1988 Jul 18;234(2):435-8. doi: 10.1016/0014-5793(88)80132-7.
2
Regulation of the actin-activated ATPase activity of Acanthamoeba myosin II by copolymerization with phosphorylated and dephosphorylated peptides derived from the carboxyl-terminal end of the heavy chain.通过与源自重链羧基末端的磷酸化和去磷酸化肽共聚来调节棘阿米巴肌球蛋白II的肌动蛋白激活的ATP酶活性。
J Biol Chem. 1990 Jun 15;265(17):9993-8.
3
Functional consequences of the proteolytic removal of regulatory serines from the nonhelical tailpiece of Acanthamoeba myosin II.从棘阿米巴肌球蛋白II的非螺旋尾段蛋白水解去除调节性丝氨酸的功能后果。
Biochemistry. 1990 Apr 17;29(15):3793-7. doi: 10.1021/bi00467a028.
4
Filament formation and actin-activated ATPase activity are abolished by proteolytic removal of a small peptide from the tip of the tail of the heavy chain of Acanthamoeba myosin II.通过蛋白水解从棘阿米巴肌球蛋白II重链尾部末端去除一个小肽段,可消除丝状物形成和肌动蛋白激活的ATP酶活性。
J Biol Chem. 1985 Feb 10;260(3):1967-72.
5
Cooperative dependence of the actin-activated Mg2+-ATPase activity of Acanthamoeba myosin II on the extent of filament phosphorylation.棘阿米巴肌球蛋白II的肌动蛋白激活的Mg2+ -ATP酶活性对细丝磷酸化程度的协同依赖性。
J Biol Chem. 1989 Mar 5;264(7):4127-32.
6
A model for the polymerization of Acanthamoeba myosin II and the regulation of its actin-activated Mg2+-ATPase activity.棘阿米巴肌球蛋白II聚合及其肌动蛋白激活的Mg2+ -ATP酶活性调节的模型。
J Biol Chem. 1987 Nov 15;262(32):15809-11.
7
Purification and characterization of a third isoform of myosin I from Acanthamoeba castellanii.来自卡氏棘阿米巴的肌球蛋白I第三种同工型的纯化与鉴定
J Biol Chem. 1989 Nov 15;264(32):19333-9.
8
Structure-function studies on Acanthamoeba myosins IA, IB, and II.棘阿米巴肌球蛋白IA、IB和II的结构-功能研究
J Cell Biochem. 1988 Jan;36(1):37-50. doi: 10.1002/jcb.240360105.
9
Regulation of the actin-activated ATPase and in vitro motility activities of monomeric and filamentous Acanthamoeba myosin II.棘阿米巴肌球蛋白II单体和丝状肌动蛋白激活的ATP酶及体外运动活性的调节
J Biol Chem. 1992 Oct 15;267(29):20900-4.
10
The effect of actin and phosphorylation on the tryptic cleavage pattern of Acanthamoeba myosin IA.肌动蛋白和磷酸化对棘阿米巴肌球蛋白IA胰蛋白酶切割模式的影响。
J Biol Chem. 1989 Jun 15;264(17):10243-50.

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