Morrison S Shawn, Mullineaux Conrad W, Ashby Mark K
Department of Basic Medical Sciences, Biochemistry Section, the University of the West Indies, Mona Campus, Kingston 7, Jamaica.
BMC Microbiol. 2005 Aug 2;5:47. doi: 10.1186/1471-2180-5-47.
The dspA (hik33) gene, coding for a putative sensory histidine kinase, is conserved in plastids (ycf26) and cyanobacteria. It has been linked with a number of different stress responses in cyanobacteria.
We constructed an insertional mutant of dspA (ycf26) in Synechocystis 6803. We found little phenotypic effect during nitrogen starvation. However, when the mutation was combined with deletion of the pta gene coding for phosphotransacetylase, a more significant phenotype was observed. Under nitrogen starvation, the pta/dspA double mutant degrades its phycobilisomes less than the wild type and still has about half of its chlorophyll-protein complexes.
Our data indicates that acetyl-phosphate-dependent phosphorylation of response regulator(s) overlaps with DspA-dependent signalling of the degradation of chlorophyll-protein complexes (and to a lesser extent phycobilisomes) in Synechocystis 6803.
编码假定的传感组氨酸激酶的dspA(hik33)基因在质体(ycf26)和蓝细菌中保守。它与蓝细菌中的许多不同应激反应有关。
我们构建了集胞藻6803中dspA(ycf26)的插入突变体。我们发现在氮饥饿期间几乎没有表型效应。然而,当该突变与编码磷酸转乙酰酶的pta基因缺失相结合时,观察到更显著的表型。在氮饥饿条件下,pta/dspA双突变体比野生型降解其藻胆体的程度更低,并且仍保留约一半的叶绿素-蛋白复合物。
我们的数据表明,响应调节因子的乙酰磷酸依赖性磷酸化与集胞藻6803中叶绿素-蛋白复合物(以及在较小程度上藻胆体)降解的DspA依赖性信号传导重叠。