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Comparative Analysis of CPI-Motif Regulation of Biochemical Functions of Actin Capping Protein.
Biochemistry ( IF 2.9 ) Pub Date : 2020-03-10 , DOI: 10.1021/acs.biochem.0c00092
Patrick McConnell 1 , Marlene Mekel 1 , Alexander G Kozlov 1 , Olivia L Mooren 1 , Timothy M Lohman 1 , John A Cooper 1
Affiliation  

The heterodimeric actin capping protein (CP) is regulated by a set of proteins that contain CP-interacting (CPI) motifs. Outside of the CPI motif, the sequences of these proteins are unrelated and distinct. The CPI motif and surrounding sequences are conserved within a given protein family, when compared to those of other CPI-motif protein families. Using biochemical assays with purified proteins, we compared the ability of CPI-motif-containing peptides from different protein families (a) to bind to CP, (b) to allosterically inhibit barbed-end capping by CP, and (c) to allosterically inhibit interaction of CP with V-1, another regulator of CP. We found large differences in potency among the different CPI-motif-containing peptides, and the different functional assays showed different orders of potency. These biochemical differences among the CPI-motif peptides presumably reflect interactions between CP and CPI-motif peptides involving amino acid residues that are conserved but are not part of the strictly defined consensus, as it was originally identified in comparisons of sequences of CPI motifs across all protein families [Hernandez-Valladares, M., et al. (2010) Structural characterization of a capping protein interaction motif defines a family of actin filament regulators. Nat. Struct. Mol. Biol. 17, 497-503; Bruck, S., et al. (2006) Identification of a Novel Inhibitory Actin-capping Protein Binding Motif in CD2-associated Protein. J. Biol. Chem. 281, 19196-19203]. These biochemical differences may be important for conserved distinct functions of CPI-motif protein families in cells with respect to the regulation of CP activity and actin assembly near membranes.

中文翻译:

肌动蛋白封端蛋白生化功能的CPI基调调控的比较分析。

异二聚肌动蛋白封端蛋白(CP)由一组包含CP相互作用(CPI)图案的蛋白调节。在CPI基序之外,这些蛋白质的序列无关且不同。与其他CPI基序蛋白家族的那些相比,CPI基序和周围序列在给定的蛋白家族中是保守的。使用纯化蛋白的生化分析,我们比较了来自不同蛋白家族的含CPI基序的肽的能力(a)结合CP,(b)变构抑制CP的带刺末端封端,和(c)变构抑制CP与CP的另一个调节器V-1的交互作用。我们发现不同的包含CPI基元的肽段在效能上有很大差异,并且不同的功能测定显示出不同的效能等级。CPI基序肽之间的这些生化差异可能反映了CP和CPI基序肽之间的相互作用,涉及保守但不属于严格定义的氨基酸残基的氨基酸残基,因为最初是在比较所有CPI基序序列时发现的蛋白质家族[Hernandez-Valladares,M.等。(2010)封盖蛋白相互作用基序的结构表征定义了肌动蛋白丝调节剂家族。纳特 结构。大声笑 生物学 17,497-503;Bruck,S。等。(2006)CD2相关蛋白中新型抑制性肌动蛋白上限蛋白结合基序的鉴定。J.Biol。化学 281,19196-19203]。
更新日期:2020-03-10
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