Sgt1p在芽殖酵母中对环磷酸腺苷（cAMP）信号通路活性有贡献，并与腺苷酸环化酶Cyr1p/Cdc35p发生物理相互作用。
Sgt1p contributes to cyclic AMP pathway activity and physically interacts with the adenylyl cyclase Cyr1p/Cdc35p in budding yeast.
作者信息
Dubacq Caroline, Guerois Raphaël, Courbeyrette Régis, Kitagawa Katsumi, Mann Carl
机构信息
Service de Biochimie et de Génétique Moléculaire, CEA/Saclay, F-91191 Gif-sur-Yvette, France.
出版信息
Eukaryot Cell. 2002 Aug;1(4):568-82. doi: 10.1128/EC.1.4.568-582.2002.
Abstract
Sgt1p is a highly conserved eucaryotic protein that is required for both SCF (Skp1p/Cdc53p-Cullin-F-box)-mediated ubiquitination and kinetochore function in yeast. We show here that Sgtlp is also involved in the cyclic AMP (cAMP) pathway in Saccharomyces cerevisiae. SGT1 is an allele-specific suppressor of cdc35-1, a thermosensitive mutation in the leucine-rich repeat domain of the adenylyl cyclase Cyrlp/Cdc35p. We demonstrate that Sgt1p and Cyrlp/Cdc35p physically interact and that the activity of the cAMP pathway is affected in an sgt1 conditional mutant. Sequence analysis suggests that Sgtlp has features of a cochaperone. Thus, Sgt1p is a novel activator of adenylyl cyclase in S. cerevisiae and may function in the assembly or the conformational activation of specific multiprotein complexes.
摘要
Sgt1p是一种高度保守的真核蛋白，在酵母中，它对于SCF（Skp1p/Cdc53p-遍在蛋白连接酶骨架蛋白-F盒蛋白）介导的泛素化作用和动粒功能均是必需的。我们在此表明，Sgtlp也参与酿酒酵母中的环磷酸腺苷（cAMP）途径。SGT1是cdc35-1的等位基因特异性抑制子，cdc35-1是腺苷酸环化酶Cyrlp/Cdc35p富含亮氨酸重复结构域中的一个温度敏感型突变。我们证明Sgt1p与Cyrlp/Cdc35p存在物理相互作用，并且在sgt1条件突变体中cAMP途径的活性受到影响。序列分析表明Sgtlp具有共伴侣蛋白的特征。因此，Sgt1p是酿酒酵母中腺苷酸环化酶的一种新型激活剂，可能在特定多蛋白复合物的组装或构象激活中发挥作用。
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