Institute of Plant Biology, Biological Research Center, Hungarian Academy of Sciences, Temesvári krt. 62, H-6726 Szeged, Hungary.
Plant Physiol Biochem. 2012 Mar;52:162-8. doi: 10.1016/j.plaphy.2011.12.010. Epub 2012 Jan 10.
SET/I(2)(PP2A), a member of the family of nucleosome assembly proteins (NAPs), has been previously described as a multifunctional protein inhibiting protein phosphatase 2A (PP2A)-mediated histone H3((pSer10)) dephosphorylation during the heat shock response in animal cells. In the present work we demonstrate that its plant orthologs, designated as NAP-related proteins (NRPs), have a similar in vitro biochemical activity and interact with PP2A and histone H3((pSer10))in vivo. Although heat shock gene promoters were found to be associated with histone H3((pSer10))-marked chromatin following a high temperature treatment, heat shock gene expression was not affected in NRP-deficient mutant Arabidopsis thaliana (L.) plantlets. These observations indicate that NRPs are potential regulators of histone dephosphorylation in plants, but they are dispensable for gene expression reorganization in response to heat shock.
SET/I(2)(PP2A) 是核小体装配蛋白(NAPs)家族的成员,先前被描述为一种多功能蛋白,可在动物细胞的热休克反应中抑制蛋白磷酸酶 2A(PP2A)介导的组蛋白 H3((pSer10))去磷酸化。在本工作中,我们证明其植物直系同源物,称为 NAP 相关蛋白(NRPs),具有相似的体外生化活性,并与 PP2A 和组蛋白 H3((pSer10))在体内相互作用。尽管在高温处理后发现热休克基因启动子与组蛋白 H3((pSer10))标记的染色质相关,但在 NRP 缺陷型拟南芥突变体植物中,热休克基因表达并未受到影响。这些观察结果表明,NRPs 是植物中组蛋白去磷酸化的潜在调节剂,但它们对于热休克响应中基因表达的重新组织是可有可无的。