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一种新型cGMP磷酸二酯酶的鉴定,该酶在趋化性stmF突变体中存在缺陷。

Identification of a novel type of cGMP phosphodiesterase that is defective in the chemotactic stmF mutants.

作者信息

Meima Marcel E, Biondi Ricardo M, Schaap Pauline

机构信息

School of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.

出版信息

Mol Biol Cell. 2002 Nov;13(11):3870-7. doi: 10.1091/mbc.e02-05-0285.

Abstract

StmF mutants are chemotactic mutants that are defective in a cGMP phosphodiesterase (PDE) activity. We identified a novel gene, PdeD, that harbors two cyclic nucleotide-binding domains and a metallo-beta-lactamase homology domain. Similar to stmF mutants, pdeD-null mutants displayed extensively streaming aggregates, prolonged elevation of cGMP levels after chemotactic stimulation, and reduced cGMP-PDE activity. PdeD transcripts were lacking in stmF mutant NP377, indicating that this mutant carries a PdeD lesion. Expression of a PdeD-YFP fusion protein in pdeD-null cells restored the normal cGMP response and showed that PdeD resides in the cytosol. When purified by immunoprecipitation, the PdeD-YFP fusion protein displayed cGMP-PDE activity, which was retained in a truncated construct that contained only the metallo-beta-lactamase domain.

摘要

StmF突变体是在环鸟苷酸磷酸二酯酶(PDE)活性方面存在缺陷的趋化性突变体。我们鉴定出一个新基因PdeD,它含有两个环核苷酸结合结构域和一个金属β-内酰胺酶同源结构域。与stmF突变体相似,pdeD基因缺失突变体表现出广泛的流动聚集体,趋化刺激后cGMP水平的持续升高,以及cGMP-PDE活性降低。stmF突变体NP377中缺乏PdeD转录本,表明该突变体存在PdeD损伤。在pdeD基因缺失的细胞中表达PdeD-YFP融合蛋白可恢复正常的cGMP反应,并表明PdeD定位于细胞质中。通过免疫沉淀纯化时,PdeD-YFP融合蛋白表现出cGMP-PDE活性,该活性保留在仅包含金属β-内酰胺酶结构域的截短构建体中。

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