Cpc1, a Chlamydomonas central pair protein with an adenylate kinase domain
Cpc1, a Chlamydomonas central pair protein with an adenylate kinase domain
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DOI：
10.1242/jcs.01297
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发表时间：
2004-08
影响因子：
4
通讯作者：
Hui Zhang;D. Mitchell
中科院分区：
文献类型：
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作者：
Hui Zhang;D. Mitchell
突变在CPC 1破坏组装的一个中央对微管相关的复合物和改变鞭毛节拍频率在衣原体。互补cpc 1的野生型基因组克隆和相应cDNA的序列揭示了该基因产物是具有两个预测功能域的205 kDa蛋白质，一个靠近C-末端的单EF手基序和一个不寻常的位于中心的腺苷酸激酶结构域。同源物在哺乳动物（睾丸和气管纤毛）以及纤毛低等真核生物中表达。Western印迹证实Cpc 1是16 S中心配对相关复合物中的六个亚基之一。运动缺陷与cpc 1等位基因在体内部分获救，在体外的轴丝或细胞模型在饱和浓度的ATP的重新激活，因此，cpc 1复合物是必不可少的，以维持正常的ATP浓度在鞭毛。
Mutations at CPC1 disrupt assembly of a central pair microtubule-associated complex and alter flagellar beat frequency in Chlamydomonas. Sequences of wild-type genomic clones that complement cpc1, and of corresponding cDNAs, reveal the gene product to be a 205 kDa protein with two predicted functional domains, a single EF hand motif near the C-terminus and an unusual centrally located adenylate kinase domain. Homologs are expressed in mammals (testis and tracheal cilia) as well as ciliated lower eukaryotes. Western blots confirm that Cpc1 is one of six subunits in a 16S central pair-associated complex. Motility defects associated with cpc1 alleles in vivo are partially rescued in vitro by reactivation of axonemes or cell models in saturating concentrations of ATP; thus the Cpc1 complex is essential for maintaining normal ATP concentrations in the flagellum.