The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts
The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts
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DOI：
10.1007/s00294-002-0309-8
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发表时间：
2002-07
期刊：
影响因子：
2.5
通讯作者：
A. Sokolenko;E. Pojidaeva;V. Zinchenko;V. Panichkin;V. Glaser;R. Herrmann;S. Shestakov
中科院分区：
文献类型：
--
作者：
A. Sokolenko;E. Pojidaeva;V. Zinchenko;V. Panichkin;V. Glaser;R. Herrmann;S. Shestakov
一组62个基因编码集胞藻的整个肽酶补体。PCC 6803已在该蓝细菌的基因组数据库中被鉴定出来。与蓝细菌基因组的序列比较揭示了从蓝细菌祖先遗传的可能同源的叶绿体成分。一个系统的基因破坏方法被选择单独地破坏，由习惯的转化策略，大多数的蓝藻基因编码的肽酶亚基，叶绿体酶。这允许分类的肽酶，细胞活力所需的或参与特定的应激反应。对集胞藻和裸藻叶绿体肽酶的比较分析表明：（1）在蓝细菌中由基因复制产生的同源酶在功能上是多样的，并且经常不相互补充，（2）叶绿体似乎含有许多不同的蓝藻来源的肽酶多肽链（49），这与蓝藻细胞（62）和（3）相当。质体中的肽酶补体是由某些蓝细菌肽酶的损失和肽酶亚类的获得或多样化的组合引起的。蛋白水解酶模式的这种重组可能反映了原核和细胞器系统之间不同的环境和生理变化。
A set of 62 genes that encode the entire peptidase complement ofSynechocystissp. PCC 6803 has been identified in the genome database of that cyanobacterium. Sequence comparisons with theArabidopsisgenome uncovered the presumably homologous chloroplast components inherited from their cyanobacterial ancestor. A systematic gene disruption approach was chosen to individually inactivate, by customary transformation strategies, the majority of the cyanobacterial genes encoding peptidase subunits that are related to chloroplast enzymes. This allowed classification of the peptidases that are required for cell viability or are involved in specific stress responses. The comparative analysis betweenSynechocystisandArabidopsischloroplast peptidases showed that: (1) homologous enzymes that arose by gene duplications in cyanobacteria are functionally diverse and frequently do not complement each other, (2) the chloroplast appears to house a number of distinct peptidase polypeptide chains of cyanobacterial origin (49) which is comparable with a cyanobacterial cell (62) and (3) the peptidase complement in plastids results from a combination of the loss of some cyanobacterial peptidases and the gain or diversification of subclasses of peptidases. This reorganization in the pattern of proteolytic enzymes may reflect distinct environmental and physiological changes between prokaryotic and organellar systems.