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-Structure paper
タイトル | Oligomerization of plant FtsZ1 and FtsZ2 plastid division proteins. |
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ジャーナル・号・ページ | Arch Biochem Biophys, Vol. 513, Issue 2, Page 94-9101, Year 2011 |
掲載日 | 2011年9月15日 |
著者 | Aaron G Smith / Carol B Johnson / Stanislav Vitha / Andreas Holzenburg / |
PubMed 要旨 | FtsZ was identified in bacteria as the first protein to localize mid-cell prior to division and homologs have been found in many plant species. Bacterial studies demonstrated that FtsZ forms a ring ...FtsZ was identified in bacteria as the first protein to localize mid-cell prior to division and homologs have been found in many plant species. Bacterial studies demonstrated that FtsZ forms a ring structure that is dynamically exchanged with a soluble pool of FtsZ. Our previous work established that Arabidopsis FtsZ1 and FtsZ2-1 are capable of in vitro self-assembly into two distinct filament types, termed type-I and type-II and noted the presence of filament precursor molecules which prompted this investigation. Using a combination of electron microscopy, gel chromatography and native PAGE revealed that (i) prior to FtsZ assembly initiation the pool consists solely of dimers and (ii) during assembly of the Arabidopsis FtsZ type-II filaments the most common intermediate between the dimer and filament state is a tetramer. Three-dimensional reconstructions of the observed dimer and tetramer suggest these oligomeric forms may represent consecutive steps in type-II filament assembly and a mechanism is proposed, which is expanded to include FtsZ assembly into type-I filaments. Finally, the results permit a discussion of the oligomeric nature of the soluble pool in plants. |
リンク | Arch Biochem Biophys / PubMed:21781955 |
手法 | EM (単粒子) |
解像度 | 25.0 Å |
構造データ | EMDB-1910: EMDB-1911: |
由来 |
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