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首页> 外文期刊>Cellular Signalling >Mkp1 of Pneumocystis carinii associates with the yeast transcription factor Rlm1 via a mechanism independent of the activation state
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Mkp1 of Pneumocystis carinii associates with the yeast transcription factor Rlm1 via a mechanism independent of the activation state

机译：卡氏肺孢子虫的Mkp1通过独立于激活状态的机制与酵母转录因子Rlm1相关联

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摘要

The mitogen-activated protein (MAP) kinase Mkp1 of the fungal pathogen Pneumocystis carinii is a functional MAP kinase that complements the loss of Slt2p, the MAP kinase component of the cen integrity pathway of Saccharomyces cerevisiae, and is activated within P. carinii in response to oxidative stress. Mkp1 displays an unusual feature in that it contains a phosphorylation motif repeat (TEYMTEY) within the activation loop not present in any other fungal MAPK identified to date. Mutagenesis of the T186,Y188 phosphorylation motif within the activation domain of Mkp1 results in the loss of detectable kinase activity but still retains partial complementation function. In addition to the ability of Mkp1 to restore partial activity to the cell integrity pathway in the absence of phosphorylatable residues within the activation loop, the association of Mkp1 with a substrate of Slt2p. the transcription factor Rlm1p, can also occur in the absence of MAP kinase activation. The results of this study suggest that the presence of phosphorylatable residues within the activation loop of Mkp1 is not absolutely required for functional (complementation) activity or for the association of Mkp1 with the transcription factor Rlm1p. In contrast, the catalytic lysine of the ATP-binding domain of Mkp1 is necessary for both complementation function and interaction with Rlm1p. (C) 2000 Elsevier Science Inc. All rights reserved. [References: 40]
机译：真菌病原体卡氏肺孢子虫的促分裂原活化蛋白（MAP）激酶Mkp1是一种功能性MAP激酶，可补充啤酒酵母cen完整性途径的Slt2p的MAP激酶成分Slt2p的丢失，并在卡氏疟原虫中响应而被激活。氧化应激。 Mkp1显示一个不寻常的功能，因为它在激活环中包含一个磷酸化基序重复序列（TEYMTEY），迄今为止在鉴定的任何其他真菌MAPK中都不存在。 Mkp1激活域内的T186，Y188磷酸化基序的诱变导致可检测的激酶活性丧失，但仍保留部分互补功能。在激活环内不存在可磷酸化残基的情况下，除了Mkp1恢复细胞完整性途径的部分活性的能力外，Mkp1与Slt2p的底物也有关联。转录因子Rlm1p，也可能在没有MAP激酶激活的情况下发生。这项研究的结果表明，功能（互补）活性或Mkp1与转录因子Rlm1p的结合并不是Mkp1激活环内可磷酸化残基的绝对存在。相反，Mkp1 ATP结合域的催化赖氨酸对于互补功能和与Rlm1p的相互作用都是必需的。 （C）2000 Elsevier Science Inc.保留所有权利。 [参考：40]

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