IS THE FUNCTION OF THE CDC2 KINASE SUBUNIT PROTEINS TUNED BY THEIR PROPENSITIES TO OLIGOMERIZE - CONFORMATIONAL STATES IN SOLUTION OF THE CDC2 KINASE PARTNERS P13(SUCL) AND P9(CKSPHY)

Birck C; Vachette P; Welch M; Swaren P; Samama JP

首页> 外文期刊>Biochemistry >IS THE FUNCTION OF THE CDC2 KINASE SUBUNIT PROTEINS TUNED BY THEIR PROPENSITIES TO OLIGOMERIZE - CONFORMATIONAL STATES IN SOLUTION OF THE CDC2 KINASE PARTNERS P13(SUCL) AND P9(CKSPHY)

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IS THE FUNCTION OF THE CDC2 KINASE SUBUNIT PROTEINS TUNED BY THEIR PROPENSITIES TO OLIGOMERIZE - CONFORMATIONAL STATES IN SOLUTION OF THE CDC2 KINASE PARTNERS P13(SUCL) AND P9(CKSPHY)

机译：CDC2激酶亚单位蛋白的功能是由它们的寡聚化-构象状态在CDC2激酶伴侣P13（SUCL）和P9（CKSPHY）的解决方案中所调节的

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The cdc2 kinase subunit (cks) proteins play an essential function in the control of mitosis through their molecular complexes with the cdc2 kinase. In this work, we characterize the conformational state(s) in solution of the cks proteins p13(suc1) from Schizosaccharomyces pombe and p9(cksphy) from Physarum polycephalum. Monomers of p13(suc1) and p9(cksphy) were found to be markedly nonglobular, presumably with a long, nonfolded C-terminal moiety. This was in contrast to the previously published structure of p13(suc1), derived from crystallographic studies on a zinc-promoted p13(suc1) dimer, in which the individual p13(suc1) subunits had a globular conformation. This disparity was resolved when we found that the globular p13(suc1) fold undergoes a conformational transition into nonglobular monomers upon dissociation of the dimers following chelation of the zinc ions by ethylenediaminetetraacetic acid (EDTA). We also found that p13(suc1), but not p9(cksphy), forms stable dimers in the absence of metal ions. The topology of these EDTA-insensitive dimers likely resembles that of the human p9(ckshs2) protein, characterized by beta 4 strand exchange from each nonglobular monomer.

机译：cdc2激酶亚基（cks）蛋白通过与cdc2激酶的分子复合物，在控制有丝分裂中起着至关重要的作用。在这项工作中，我们表征了粟酒裂殖酵母的cks蛋白p13（suc1）和多头Phys骨的p9（cksphy）溶液的构象状态。发现p13（suc1）和p9（cksphy）的单体明显呈非球形，推测具有长的，未折叠的C端部分。这与先前公布的p13（suc1）结构相反，该结构是从锌促进的p13（suc1）二聚体的晶体学研究得出的，其中单个p13（suc1）亚基具有球状构象。当我们发现在乙二胺四乙酸（EDTA）螯合锌离子后，二聚体解离后，球形p13（suc1）折叠发生构象转变为非球形单体，这种差异得以解决。我们还发现，在没有金属离子的情况下，p13（suc1）而非p9（cksphy）形成稳定的二聚体。这些EDTA不敏感的二聚体的拓扑结构可能类似于人p9（ckshs2）蛋白的拓扑结构，其特征是每个非球状单体的β4链交换。

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《Biochemistry》 |1996年第17期|共9页
作者
Birck C; Vachette P; Welch M; Swaren P; Samama JP;
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正文语种 eng
中图分类生物化学;
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Cyclin-dependent kinases; Fission yeast; Cell-cycle; Schizosaccharomyces-pombe; Saccharomyces-cerevisiae; Division cycle; Activation; P34cdc2; P13suc1; Suc1;

机译：细胞周期蛋白依赖性激酶;裂变酵母;细胞周期;裂殖酵母;酿酒酵母;分裂周期;激活;P34cdc2;P13suc1;Suc1;

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1. IS THE FUNCTION OF THE CDC2 KINASE SUBUNIT PROTEINS TUNED BY THEIR PROPENSITIES TO OLIGOMERIZE - CONFORMATIONAL STATES IN SOLUTION OF THE CDC2 KINASE PARTNERS P13(SUCL) AND P9(CKSPHY) [J] . Birck C, Vachette P, Welch M, Biochemistry . 1996,第17期

机译：CDC2激酶亚单位蛋白的功能是由它们的寡聚化-构象状态在CDC2激酶伴侣P13（SUCL）和P9（CKSPHY）的解决方案中所调节的
2. The consensus sequences for cdc2 kinase and for casein kinase‐2 are mutually incompatible A study with peptides derived from the β‐subunit of casein kinase‐2 [J] . Draetta Giulio, Marin Oriano, Meggio Flavio, FEBS Letters . 1992,第1期

机译：cdc2激酶和酪蛋白激酶-2的共有序列互不兼容一项关于酪蛋白激酶-2β亚基衍生肽的研究
3. New Cdc2 Tyr 4 phosphorylation by dsRNA-activated protein kinase triggers Cdc2 polyubiquitination and G2 arrest under genotoxic stresses [J] . Yoon CH, Miah MA, Kim KP, EMBO reports . 2010,第5期

机译：dsRNA激活的蛋白激酶将新的Cdc2 Tyr 4磷酸化引发Cdc2多聚泛素化和G2在基因毒性胁迫下停滞
4. Structural insights into conformational flexibility ofcAMP-dependent protein kinase from the unliganded and liganded catalytic subunit. [D] . Akamine, Pearl Yoshimi. 2002

机译：来自未配体和配体催化亚基的cAMP依赖性蛋白激酶构象柔性的结构见解。
5. The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues. [O] . D Fesquet, J C Labbé, J Derancourt, 1993

机译：MO15基因编码蛋白激酶的催化亚基该蛋白激酶通过Thr161及其同系物的磷酸化激活cdc2和其他细胞周期蛋白依赖性激酶（CDK）。
6. The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues. [O] . Fesquet D, Labbé J C, Derancourt J, 1993

机译：MO15基因编码蛋白激酶的催化亚基，该蛋白激酶通过Thr161及其同系物的磷酸化激活cdc2和其他细胞周期蛋白依赖性激酶（CDK）。
7. Solution structure analysis of the conformational changes that occur upon the binding of the protein kinase inhibitor peptide to the catalytic subunit of the cAMP dependent protein kinase [R] . Mitchell, R. D. , Walsh, D. A. , Olah, G. A. , 1994

机译：蛋白激酶抑制剂肽与camp依赖性蛋白激酶催化亚基结合后发生的构象变化的溶液结构分析

IS THE FUNCTION OF THE CDC2 KINASE SUBUNIT PROTEINS TUNED BY THEIR PROPENSITIES TO OLIGOMERIZE - CONFORMATIONAL STATES IN SOLUTION OF THE CDC2 KINASE PARTNERS P13(SUCL) AND P9(CKSPHY)

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