Acclimation to low [CO2] by an inorganic carbon-concentrating mechanism in Cyanophora paradoxa

Acclimation to low [CO2] by an inorganic carbon-concentrating mechanism in Cyanophora paradoxa
复制标题

DOI:
10.1111/j.1365-3040.2007.01715.x
复制
发表时间:
2007-11-01
影响因子:
7.3
通讯作者:
Loeffelhardt, W.
Loeffelhardt, W.
中科院分区:
生物学1区
文献类型:
--
作者:
Burey, S. C.;Poroyko, V.;Loeffelhardt, W.

文献摘要

被引文献

相似文献

蓝囊藻含有蓝色素,具有原核分裂特征的质体,如肽聚糖壁和中心蛋白质包涵体。虽然该中心体包括大部分的酶核酮糖1,5-二磷酸羧化酶/氧合酶Rubisco),但C. paradox悖论has only been hypothesized假设.在这里,我们提出的生理数据支持CCM:CO2交换活性以及对无机碳的表观亲和力被发现增加CO2限制应力下。此外,表达序列标签(EST)的C。从两个cDNA文库中获得了paradoxa,一个来自在高[CO2]条件下生长的细胞,一个来自在低[CO2]条件下生长的细胞。从2378个cDNA序列组装的cDNA微阵列平台显示,142个基因显着响应从高到低[CO2]的转变。基因表达的趋势与莱茵衣藻和蓝藻集胞藻6803(两者均具有CCM)的报告结果相当。在受[CO2]调控的基因中,在C. paradoxa,可能在CCM中起作用。这些结果和多面体外观的中央机构进一步支持的假说,一个独特的“真核羧基”的蓝藻。
The glaucocystophyte Cyanophora paradoxa contains cyanelles, plastids with prokaroytic features such as a peptidoglycan wall and a central proteinaceous inclusion body. While this central body includes the majority of the enzyme ribulose 1,5-bisphosphate carboxylase/oxgenase Rubisco), the presence of a carbon-concentrating mechanism (CCM) in C. paradoxa has only been hypothesized. Here, we present physiological data in support of a CCM: CO2 exchange activity as well as apparent affinity against inorganic carbon were found to increase under CO2-limiting stress. Further, expressed sequence tags (ESTs) of C. paradoxa were obtained from two cDNA libraries, one from cells grown in high [CO2] conditions and one from cells grown under low [CO2] conditions. A cDNA microarray platform assembled from 2378 cDNA sequences revealed that 142 genes significantly responded to a shift from high to low [CO2]. Trends in gene expression were comparable to those reported for Chlamydomonas reinhardtii and the cyanobacterium Synechocystis 6803, both possessing a CCM. Among genes regulated by [CO2], transcripts were identified encoding carbonic anhydrases (CAs), Rubisco activase and a putative bicarbonate transporter in C. paradoxa, likely functionally involved in the CCM. These results and the polyhedric appearance of the central body further support the hypothesis of a unique 'eukaryotic carboxysome' in Cyanophora.