Plasticity of the domain structure in FlgJ, a bacterial protein involved in flagellar rod formation
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- Nambu Takayuki
- Department of Bioscience, Nagahama Institute of Bioscience and Technology
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- Inagaki Yuji
- Center for Computational Sciences and Institute of Biological Sciences, University of Tsukuba
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- Kutsukake Kazuhiro
- Graduate School of Natural Science and Technology and Department of Biology, Faculty of Science, Okayama University
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Bacterial flagellar rod structure is built across the peptidoglycan (PG) layer. A Salmonella enterica flagellar protein FlgJ is believed to consist of two functional domains, the N-terminal half acting as a scaffold or cap essential for rod assembly and the C-terminal half acting as a PG hydrolase (PGase) that makes a hole in the PG layer to facilitate rod penetration. In this study, molecular data analyses were conducted on FlgJ data sets sampled from a variety of bacterial species, and three types of FlgJ homologs were identified: (i) “canonical dual-domain” type found in β- and γ-proteobacteria that has a domain for one of the PGases, acetylmuramidase (Acm), at the C terminus, (ii) “non-canonical dual-domain” type found in the genus Desulfovibrio (δ-proteobacteria) that bears a domain for another PGase, M23/M37-family peptidase (Pep), at the C terminus and (iii) “single-domain” type found in phylogenetically diverged lineages that lacks the Acm or Pep domain. FlgJ phylogeny, together with the domain architecture, suggested that the single-domain type was the original form of FlgJ and the canonical dual-domain type had evolved from the single-domain type by fusion of the Acm domain to its C terminus in the common ancestor of β- and γ-proteobacteria. The non-canonical dual-domain type may have been formed by fusion of the Pep domain to the single-domain type in the ancestor of Desulfovibrio. In some lineages of γ-proteobacteria, the Acm domain appeared to be lost secondarily from the dual-domain type FlgJ to yield again a single-domain type one. To rationalize the underlying mechanism that gave rise to the two different types of dual-domain FlgJ homologs, we propose a model assuming the lineage-specific co-option of flagellum-specific PGase from diverged housekeeping PGases in bacteria.<br>
収録刊行物
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- Genes & Genetic Systems
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Genes & Genetic Systems 81 (6), 381-389, 2006
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詳細情報 詳細情報について
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- CRID
- 1390001205473617024
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- NII論文ID
- 10018827975
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- NII書誌ID
- AA11077421
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- ISSN
- 18805779
- 13417568
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- NDL書誌ID
- 8621241
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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
- Crossref
- CiNii Articles
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- 使用不可