Landrieu I, De Veylder L, Fruchart J S, Odaert B, Casteels P, Portetelle D, Van Montagu M, Inzé D, Lippens G
Unité de Microbiologie, Faculté Universitaire des Sciences Agronomiques de Gembloux, B-5030 Gembloux, Belgium.
J Biol Chem. 2000 Apr 7;275(14):10577-81. doi: 10.1074/jbc.275.14.10577.
A homologue of the human site-specific prolyl cis/trans isomerase PIN1 was identified in Arabidopsis thaliana. The PIN1At gene encodes a protein of 119 amino acids that is 53% identical with the catalytic domain of the human PIN1 parvulin. Steady-state PIN1At mRNA is found in all plant tissues tested. We show by two-dimensional NMR spectroscopy that the PIN1At is a prolyl cis/trans isomerase with specificity for phosphoserine-proline bonds. PIN1At is the first example of an eukaryotic parvulin without N- or C-terminal extensions. The N-terminal WW domain of 40 amino acids, typical of all the phosphorylation-dependent eukaryotic parvulins, is absent. However, triple-resonance NMR experiments showed that PIN1At contained a hydrophobic helix similar to the alpha1 helix observed in PIN1 that could mediate the protein-protein interactions.
在拟南芥中鉴定出了人类位点特异性脯氨酰顺反异构酶PIN1的同源物。PIN1At基因编码一种由119个氨基酸组成的蛋白质，该蛋白质与人类PIN1 parvulin的催化结构域有53%的同一性。在所有测试的植物组织中均发现了稳态PIN1At mRNA。我们通过二维核磁共振光谱表明，PIN1At是一种对磷酸丝氨酸-脯氨酸键具有特异性的脯氨酰顺反异构酶。PIN1At是没有N端或C端延伸的真核parvulin的首个例子。所有依赖磷酸化的真核parvulin典型的40个氨基酸的N端WW结构域不存在。然而，三共振核磁共振实验表明，PIN1At包含一个类似于在PIN1中观察到的α1螺旋的疏水螺旋，该螺旋可介导蛋白质-蛋白质相互作用。
