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通过去除紧密结合的钙离子使肌动蛋白硫醇暴露。

Exposure of actin thiols by the removal of tightly held calcium ions.

作者信息

Konno K, Morales M F

出版信息

Proc Natl Acad Sci U S A. 1985 Dec;82(23):7904-8. doi: 10.1073/pnas.82.23.7904.

DOI:10.1073/pnas.82.23.7904
PMID:3865205
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC390878/
Abstract

The removal of bound metal ions from G-actin uncovered two thiols, Cys-10 and Cys-257. The uncovering of these thiols requires a free calcium concentration lower than 10 nM. Therefore, participation of one or both thiols in Ca2+ binding is suggested. Actin labeled with N-(5-fluoresceinyl)maleimide in the absence of calcium moves as a doublet in NaDodSO4/PAGE. It is suggested that two conformers are induced by metal removal and labeling.

摘要

从G-肌动蛋白中去除结合的金属离子后发现了两个巯基,即半胱氨酸-10和半胱氨酸-257。这些巯基的暴露需要游离钙浓度低于10 nM。因此,提示一个或两个巯基参与了Ca2+结合。在没有钙的情况下用N-(5-荧光素基)马来酰亚胺标记的肌动蛋白在NaDodSO4/PAGE中以双峰形式移动。提示金属去除和标记诱导了两种构象体。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/ea10a2108a7e/pnas00363-0112-h.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/cb177ed054b8/pnas00363-0111-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/6c377eaf52eb/pnas00363-0111-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/084c6d7ade97/pnas00363-0112-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/a77a7cea2c35/pnas00363-0112-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/f25b3f252d99/pnas00363-0112-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/6e9d4fe716e5/pnas00363-0112-d.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/db31af6e5daa/pnas00363-0112-g.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/ea10a2108a7e/pnas00363-0112-h.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/328fc732335d/pnas00363-0111-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/876c7f7dc7b9/pnas00363-0111-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/cb177ed054b8/pnas00363-0111-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/6c377eaf52eb/pnas00363-0111-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/084c6d7ade97/pnas00363-0112-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/a77a7cea2c35/pnas00363-0112-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/f25b3f252d99/pnas00363-0112-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/6e9d4fe716e5/pnas00363-0112-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/87124161663f/pnas00363-0112-e.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/8bfe7fada595/pnas00363-0112-f.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/db31af6e5daa/pnas00363-0112-g.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd82/390878/ea10a2108a7e/pnas00363-0112-h.jpg

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本文引用的文献

1
Tissue sulfhydryl groups.组织巯基
Arch Biochem Biophys. 1959 May;82(1):70-7. doi: 10.1016/0003-9861(59)90090-6.
2
Identification of myosin-binding sites on the actin sequence.肌动蛋白序列上肌球蛋白结合位点的鉴定。
Biochemistry. 1982 Jul 20;21(15):3654-61. doi: 10.1021/bi00258a020.
3
A fluorescent probe for conformational changes in skeletal muscle G-actin.一种用于检测骨骼肌G-肌动蛋白构象变化的荧光探针。
肌动蛋白亚结构域2构象中依赖二价阳离子、核苷酸和聚合作用的变化。
Biophys J. 1999 Jul;77(1):373-85. doi: 10.1016/S0006-3495(99)76896-7.
4
Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation.肌动蛋白和肌球蛋白中距离的荧光共振能量转移测量:批判性评估
J Muscle Res Cell Motil. 1987 Apr;8(2):97-117. doi: 10.1007/BF01753986.
5
The accessibility of the thiol groups on G- and F-actin of rabbit muscle.兔肌G-肌动蛋白和F-肌动蛋白上巯基的可及性。
Biochem J. 1990 Mar 1;266(2):453-9. doi: 10.1042/bj2660453.
6
Tightly-bound divalent cation of actin.肌动蛋白紧密结合的二价阳离子。
J Muscle Res Cell Motil. 1992 Jun;13(3):272-84. doi: 10.1007/BF01766455.
J Biol Chem. 1980 Oct 10;255(19):8991-3.
4
Examination of the intracellular ionic environment and of ionophore action by null point measurements employing the fluorescein chromophore.利用荧光发色团通过零点测量法对细胞内离子环境和离子载体作用进行检测。
J Biol Chem. 1983 May 25;258(10):6380-9.
5
Mapping of actin-binding sites on the heavy chain of myosin subfragment 1.肌球蛋白亚片段1重链上肌动蛋白结合位点的定位
Biochemistry. 1983 Mar 29;22(7):1579-85. doi: 10.1021/bi00276a009.
6
Nucleotide in monomeric actin regulates the reactivity of the thiol groups.
Biochemistry. 1984 Apr 10;23(8):1608-12. doi: 10.1021/bi00303a004.
7
On the mechanism of energy transduction in myosin subfragment 1.关于肌球蛋白亚片段1中能量转换的机制。
Proc Natl Acad Sci U S A. 1984 Apr;81(7):2060-4. doi: 10.1073/pnas.81.7.2060.
8
Proteolysis and structure of skeletal muscle actin.骨骼肌肌动蛋白的蛋白水解作用与结构
Proc Natl Acad Sci U S A. 1984 Jun;81(12):3680-4. doi: 10.1073/pnas.81.12.3680.
9
Actin-actin and actin-deoxyribonuclease I contact sites in the actin sequence.肌动蛋白序列中的肌动蛋白-肌动蛋白和肌动蛋白-脱氧核糖核酸酶I接触位点。
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10
The reaction of a positively-charged N-ethylmaleimide derivative with actin and myosin subfragment-1.
Int J Biochem. 1981;13(7):871-3. doi: 10.1016/0020-711x(81)90109-9.