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首页> 外文期刊>Cell biology international. >Interactions between the budding yeast IQGAP homologue Iqg1p and its targets revealed by a split-EGFP bimolecular fluorescence complementation assay.
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Interactions between the budding yeast IQGAP homologue Iqg1p and its targets revealed by a split-EGFP bimolecular fluorescence complementation assay.

机译：通过拆分EGFP双分子荧光互补测定揭示了出​​芽的酵母IQGAP同源物Iqg1p与它的靶标之间的相互作用。

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摘要

A split-EGFP based bimolecular fluorescence complementation (BiFC) assay has been used to detect interactions between the Saccharomyces cerevisiae cytoskeletal scaffolding protein Iqg1p and three targets: myosin essential light chain (Mlc1p), calmodulin (Cmd1p) and the small GTPase Cdc42p. The format of the BiFC assay used ensures that the proteins are expressed at wild type levels thereby avoiding artefacts due to overexpression. This is the first direct in vivo detection of these interactions; in each case, the complex is localised to discrete regions of the yeast cytoplasm. The labelling with EGFP fragments results in changes in growth kinetics, cell size and budding frequency. This is partly due to the reassembled EGFP locking the complexes into essentially permanent interactions. The consequences of this for Iqg1p interactions and BiFC assays in general are discussed.
机译：基于分裂EGFP的双分子荧光互补（BiFC）分析已用于检测酿酒酵母细胞骨架支架蛋白Iqg1p与三个靶标之间的相互作用：肌球蛋白必需轻链（Mlc1p），钙调蛋白（Cmd1p）和小GTPase Cdc42p。所用BiFC分析的形式可确保蛋白质在野生型水平上表达，从而避免了由于过表达引起的假象。这是这些相互作用的首次体内直接检测。在每种情况下，复合物都位于酵母细胞质的离散区域。用EGFP片段标记会导致生长动力学，细胞大小和出芽频率发生变化。这部分是由于重新组装的EGFP将复合物锁定为基本上永久的相互作用。讨论了此对Iqg1p相互作用和BiFC测定的影响。

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