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鸡细胞质肌动蛋白和肌肉肌动蛋白具有不同的结构基因。

Chick cytoplasmic actin and muscle actin have different structural genes.

作者信息

Storti R V, Rich A

出版信息

Proc Natl Acad Sci U S A. 1976 Jul;73(7):2346-50. doi: 10.1073/pnas.73.7.2346.

DOI:10.1073/pnas.73.7.2346
PMID:1065885
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC430559/
Abstract

Actins isolated from embryonic chick brain and muscle differ in mobility when subjected to electrophoresis in gels containing urea and sodium dodecyl sulfate. Experiments were carried out to determine whether these actins are products of different structural genes and differ in primary amino acid sequence, or whether they are products of the same structural gene but are different because of post-translational modification. Messenger RNA from brain and muscle tissue was used to direct cell-free protein synthesis in wheat germ extracts. The synthesized actins were identified by conversion from globular to fibrous actin and by two-dimensional chromatographic analysis of tryptic peptides. The differences in electrophoretic mobility of brain compared to muscle actin were maintained in the cell-free protein synthetic products. Therefore, these mobility differences were not due to post-translational modification. It was concluded that brain and muscle actin are coded by different messenger RNAs and therefore arise from different structural genes. In addition, messenger RNA from 13- and 16-day embryonic thigh muscle directed the synthesis of both brain- and muscle-type actins, suggesting that muscle cell differentiation involves the regulation of at least two different actin genes.

摘要

从胚胎期鸡脑和肌肉中分离出的肌动蛋白,在含有尿素和十二烷基硫酸钠的凝胶中进行电泳时,迁移率有所不同。开展了实验以确定这些肌动蛋白是不同结构基因的产物且一级氨基酸序列存在差异,还是同一结构基因的产物但因翻译后修饰而有所不同。来自脑和肌肉组织的信使核糖核酸被用于指导小麦胚芽提取物中的无细胞蛋白质合成。通过从球状肌动蛋白转变为纤维状肌动蛋白以及对胰蛋白酶消化后的肽段进行二维色谱分析来鉴定合成的肌动蛋白。与肌肉肌动蛋白相比,脑肌动蛋白在电泳迁移率上的差异在无细胞蛋白质合成产物中依然存在。因此,这些迁移率差异并非由翻译后修饰导致。得出的结论是,脑肌动蛋白和肌肉肌动蛋白由不同的信使核糖核酸编码,因而源自不同的结构基因。此外,来自13日龄和16日龄胚胎大腿肌肉的信使核糖核酸指导合成了脑型和肌肉型肌动蛋白,这表明肌肉细胞分化涉及至少两个不同肌动蛋白基因的调控。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/1715bfb23a09/pnas00037-0188-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/5f3bd88e72a2/pnas00037-0186-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/b0781281f446/pnas00037-0186-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/e032fe5ec8e8/pnas00037-0186-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/dc89a97e077f/pnas00037-0187-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/1f722fc5adc1/pnas00037-0188-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/1715bfb23a09/pnas00037-0188-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/5f3bd88e72a2/pnas00037-0186-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/b0781281f446/pnas00037-0186-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/e032fe5ec8e8/pnas00037-0186-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/dc89a97e077f/pnas00037-0187-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/1f722fc5adc1/pnas00037-0188-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/529c/430559/1715bfb23a09/pnas00037-0188-b.jpg

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Chick cytoplasmic actin and muscle actin have different structural genes.鸡细胞质肌动蛋白和肌肉肌动蛋白具有不同的结构基因。
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Mammalian cytoplasmic actins are the products of at least two genes and differ in primary structure in at least 25 identified positions from skeletal muscle actins.哺乳动物细胞质肌动蛋白是至少两个基因的产物,并且在至少25个已确定的位置上,其一级结构与骨骼肌肌动蛋白不同。
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引用本文的文献

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Identification of an actin-like protein and of its messenger ribonucleic acid in Saccharomyces cerevisiae.

本文引用的文献

1
Cleavage of structural proteins during the assembly of the head of bacteriophage T4.在噬菌体T4头部组装过程中结构蛋白的切割
Nature. 1970 Aug 15;227(5259):680-5. doi: 10.1038/227680a0.
2
Messenger RNA in HeLa cells: kinetics of formation and decay.海拉细胞中的信使核糖核酸:合成与降解动力学
J Mol Biol. 1973 Aug 5;78(2):321-34. doi: 10.1016/0022-2836(73)90119-8.
3
Determination of actin messenger RNA in cultures of differentiating embryonic chick skeletal muscle.分化中的胚胎鸡骨骼肌培养物中肌动蛋白信使核糖核酸的测定
酿酒酵母中一种肌动蛋白样蛋白及其信使核糖核酸的鉴定。
J Bacteriol. 1980 Dec;144(3):1143-51. doi: 10.1128/jb.144.3.1143-1151.1980.
4
Structure of a split yeast gene: complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae.一个分裂酵母基因的结构:酿酒酵母肌动蛋白基因的完整核苷酸序列。
Proc Natl Acad Sci U S A. 1980 May;77(5):2546-50. doi: 10.1073/pnas.77.5.2546.
5
Isolation and characterization of rat skeletal muscle and cytoplasmic actin genes.大鼠骨骼肌和细胞质肌动蛋白基因的分离与鉴定
Proc Natl Acad Sci U S A. 1982 May;79(9):2763-7. doi: 10.1073/pnas.79.9.2763.
6
Construction of recombinant plasmids containing rat muscle actin and myosin light chain DNA sequences.包含大鼠肌肉肌动蛋白和肌球蛋白轻链DNA序列的重组质粒的构建。
Proc Natl Acad Sci U S A. 1980 Feb;77(2):960-4. doi: 10.1073/pnas.77.2.960.
7
Skeletal muscle actin mRNA. Characterization of the 3' untranslated region.骨骼肌肌动蛋白信使核糖核酸。3'非翻译区的特征
Nucleic Acids Res. 1981 Feb 11;9(3):579-89. doi: 10.1093/nar/9.3.579.
8
Permanently proliferating rat vascular smooth muscle cell with maintained expression of smooth muscle characteristics, including actin of the vascular smooth muscle type.具有维持平滑肌特征表达的永久性增殖大鼠血管平滑肌细胞,包括血管平滑肌型肌动蛋白。
J Cell Biol. 1980 Dec;87(3 Pt 1):594-600. doi: 10.1083/jcb.87.3.594.
9
An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins.一种能区分细胞质肌动蛋白和骨骼肌肌动蛋白的抗肌动蛋白抗体。
J Cell Biol. 1980 Sep;86(3):891-7. doi: 10.1083/jcb.86.3.891.
10
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Proc Natl Acad Sci U S A. 1980 Oct;77(10):5683-7. doi: 10.1073/pnas.77.10.5683.
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4
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5
Actin and myosin and cell movement.肌动蛋白、肌球蛋白与细胞运动。
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7
The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.兔骨骼肌收缩的调节。I. 原肌球蛋白-肌钙蛋白复合物与肌动蛋白及肌球蛋白蛋白水解片段相互作用的生化研究。
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Proc Natl Acad Sci U S A. 1974 Jun;71(6):2268-72. doi: 10.1073/pnas.71.6.2268.
9
Human heart and platelet actins are products of different genes.人类心脏肌动蛋白和血小板肌动蛋白是不同基因的产物。
Science. 1976 Jan 9;191(4222):94-5. doi: 10.1126/science.1246600.
10
Cytoplasmic nonpolysomal messenger ribonucleoprotein containing actin messenger RNA in chicken embryonic muscles.鸡胚肌肉中含肌动蛋白信使核糖核酸的细胞质非多聚核糖体信使核糖核蛋白。
Biochemistry. 1975 Aug 26;14(17):3800-7. doi: 10.1021/bi00688a012.