Structure and function of the feast/famine regulatory proteins, FFRPs
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- SUZUKI Masashi
- National Institute of Advanced Industrial Science and Technology (AIST)
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Feast/famine regulatory proteins (FFRPs) include a diverse family of transcription factors of archaea and eubacteria. The best characterized among FFRPs is E. coli Lrp (the leucine-responsive regulatory protein). A full length FFRP is composed of an N-terminal DNA-binding domain and a C-terminal assembly domain. The C-domain is involved in formation of a dimer, and higher structures (e.g. a disk composed of 4 dimers, a chromatin-like cylinder) are further assembled. A pair of DNA-binding domains in an FFRP dimer bind the DNA site NANBNCNDNETTTNENDNCNBNA, where NA and NA, e.g., are bases complementary to each other, and NE is either A or T. Such 13 bp sequences repeat with insertions of 7-8 or ∼18 basepairs in promoters regulated by FFRPs. Ligands of the size of amino acids (e.g. leucine, asparagine) signal metabolic or environmental changes directly to FFRPs by binding at the interface formed between dimers. This interaction alters the assembly form, and thus the overall DNA-binding specificity. In this way, Lrp regulates a large number of genes differently in E. coli. In Pyrococcus sp. OT3, 14 FFRPs possibly regulate many of the ∼1, 500 genes coded. It is widely believed that the common ancestor of all organisms first differentiated to archaea and eubacteria. Thus, global (i.e. genome wide) regulation by FFRPs can be the prototype of highly differentiated transcription regulatory systems found in organisms nowadays.<BR><BR>(Communicated by Masanori OTSUKA, M. J. A., Nov. 12, 2003)
収録刊行物
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- Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences
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Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences 79B (9), 274-289, 2003
日本学士院
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詳細情報 詳細情報について
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- CRID
- 1390001204145686784
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- NII論文ID
- 130000093676
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- NII書誌ID
- AA00785485
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- COI
- 1:CAS:528:DC%2BD2cXkslamuw%3D%3D
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- ISSN
- 13492896
- 03862208
- http://id.crossref.org/issn/03862208
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- NDL書誌ID
- 6837768
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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- CiNii Articles
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- 使用不可