Interaction of a phycobilisome linker polypeptide and a cyanobacterial Hsp90, HtpG
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- Sato Takeshi
- Department of molecular Biology, Fuculty of Science, Saitama Univ
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- Nakamoto Hitoshi
- Department of molecular Biology, Fuculty of Science, Saitama Univ
Bibliographic Information
- Other Title
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- フィコビリソームの骨格構造をなすリンカーポリペプチドとシアノバクテリアHsp90（HtpG）との相互作用
Description
In vivo targets of HtpG is not known, although crystal structures of domains of the E. coli HtpG have been recently determined. We showed that HtpG plays an essential role for the thermal stress management in the cyanobacterium Synechococcus sp. PCC 7942. Furthermore, we noticed reduction of phycocyanin content in the Synechococcus htpG mutant grown under normal conditions. Phycobilisome purified from the mutant by sucrose density gradient ultra-centrifugation is lighter than that from the wild type. We found that the level of the 30-kDa linker polypeptide is reduced in the mutant's phycobilisome. We over-expressed in E. coli and purified His-tagged recombinant proteins of the cyanobacterial HtpG and the linker polypeptide. The purified HtpG dimer could prevent the in vitro aggregation of the linker polypeptide at 45oC at the molar ratio of one to one. Isolation and crystallization of the HtpG/30-kDa linker polypeptide complex are in progress.
Journal
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- Plant and Cell Physiology Supplement
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Plant and Cell Physiology Supplement 2006 (0), 249-249, 2006
The Japanese Society of Plant Physiologists
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Details 詳細情報について
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- CRID
- 1390282680606491392
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- NII Article ID
- 130006990265
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- Data Source
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- JaLC
- CiNii Articles
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- Abstract License Flag
- Disallowed
