Functional alpha-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group.

Functional alpha-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group.
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大肠杆菌中产生的功能性α-原肌球蛋白。

DOI:
10.1016/s0021-9258(17)34082-6
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发表时间:
1994
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
F. Reinach
F. Reinach
中科院分区:
--
文献类型:
--
作者:
P. Monteiro;R. C. Lataro;Jesus Aparecido Ferro;F. Reinach

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与肌肉蛋白不同,在大肠杆菌中表达的α-原肌球蛋白不结合肌动蛋白,不显示头-尾聚合,并且在肌钙蛋白不存在的情况下不抑制肌动球蛋白ATP酶活性。重组和肌肉原肌球蛋白之间的唯一化学差异是重组蛋白中的第一个甲硫氨酸未被乙酰化(Hitchcock-De-Gregori,S.E.,和Heald,R. W.(1987)J.Biol.Chem.262,9730-9735)。我们在大肠杆菌中表达了三种融合原肌球蛋白。在大肠杆菌中,其氨基末端融合有2、3和17个氨基酸。所有三个融合恢复肌动蛋白结合,头-尾聚合,并抑制这些非乙酰化原肌球蛋白的肌动球蛋白ATP酶的能力。与较大的融合体不同,2和3个氨基酸的小融合体不干扰调节功能。因此,在未乙酰化的原肌球蛋白的氨基末端存在融合二肽足以取代肌肉原肌球蛋白中存在的N-乙酰基的功能。乙酰基的功能,根据我们的研究结果和卷曲螺旋结构的原肌球蛋白的结构解释。
Unlike the muscle protein, alpha-tropomyosin expressed in Escherichia coli does not bind actin, does not exhibit head-to-tail polymerization, and does not inhibit actomyosin ATPase activity in the absence of troponin. The only chemical difference between recombinant and muscle tropomyosins is that the first methionine is not acetylated in the recombinant protein (Hitchcock-De-Gregori, S.E., and Heald, R. W. (1987) J. Biol. Chem. 262, 9730-9735). We expressed three fusion tropomyosins in E. coli with 2, 3, and 17 amino acids fused to its amino terminus. All three fusions restored actin binding, head-to-tail polymerization, and the capacity to inhibit the actomyosin ATPase to these unacetylated tropomyosins. Unlike larger fusions, the small fusions of 2 and 3 amino acids do not interfere with regulatory function. Therefore the presence of a fused dipeptide at the amino terminus of unacetylated tropomyosin is sufficient to replace the function of the N-acetyl group present in muscle tropomyosin. A structural interpretation for the function of the acetyl group, based on our results and the coiled coil structure of tropomyosin, is presented.
原肌球蛋白和肌钙蛋白-原肌球蛋白对肌动球蛋白亚片段 1 ATP 酶的双重作用。
DOI: --
发表时间: 1982
期刊: The Journal of biological chemistry
影响因子: --
作者:
Lehrer,SS;Morris,EP
通讯作者: Morris,EP
在肌钙蛋白不存在和存在的情况下,原肌球蛋白氨基末端的结构对于与肌动蛋白的结合至关重要。
DOI: --
发表时间: 1988
期刊: The Journal of biological chemistry
影响因子: --
作者:
Heald,RW;Hitchcock-DeGregori,SE
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大肠杆菌中表达的鸡横纹肌 α-原肌球蛋白氨基末端变体的肌动蛋白和肌钙蛋白结合发生改变。
DOI: --
发表时间: 1987
期刊: The Journal of biological chemistry
影响因子: --
作者:
Hitchcock-DeGregori,SE;Heald,RW
通讯作者: Heald,RW
DOI: --
发表时间: 1992
期刊: The Journal of biological chemistry
影响因子: --
作者:
Hill,LE;Mehegan,JP;Butters,CA;Tobacman,LS
通讯作者: Tobacman,LS