EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Yeast rvb1 and rvb2 proteins oligomerize as a conformationally variable dodecamer with low frequency.
ジャーナル・号・ページ	J Mol Biol, Vol. 427, Issue 10, Page 1875-1886, Year 2015
掲載日	2015年5月22日
著者	Ajitha Jeganathan / Vivian Leong / Liang Zhao / Jennifer Huen / Nardin Nano / Walid A Houry / Joaquin Ortega /
PubMed 要旨	Rvb1 and Rvb2 are conserved AAA+ (ATPases associated with diverse cellular activities) proteins found at the core of large multicomponent complexes that play key roles in chromatin remodeling, ...Rvb1 and Rvb2 are conserved AAA+ (ATPases associated with diverse cellular activities) proteins found at the core of large multicomponent complexes that play key roles in chromatin remodeling, integrity of the telomeres, ribonucleoprotein complex biogenesis and other essential cellular processes. These proteins contain an AAA+ domain for ATP binding and hydrolysis and an insertion domain proposed to bind DNA/RNA. Yeast Rvb1 and Rvb2 proteins oligomerize primarily as heterohexameric rings. The six AAA+ core domains form the body of the ring and the insertion domains protrude from one face of the ring. Conversely, human Rvbs form a mixture of hexamers and dodecamers made of two stacked hexamers interacting through the insertion domains. Human dodecamers adopt either a contracted or a stretched conformation. Here, we found that yeast Rvb1/Rvb2 complexes when assembled in vivo mainly form hexamers but they also assemble as dodecamers with a frequency lower than 10%. Yeast dodecamers adopt not only the stretched and contracted structures that have been described for human Rvb1/Rvb2 dodecamers but also intermediate conformations in between these two extreme states. The orientation of the insertion domains of Rvb1 and Rvb2 proteins in these conformers changes as the dodecamer transitions from the stretched structure to a more contracted structure. Finally, we observed that for the yeast proteins, oligomerization as a dodecamer inhibits the ATPase activity of the Rvb1/Rvb2 complex. These results indicate that although human and yeast Rvb1 and Rvb2 proteins share high degree of homology, there are significant differences in their oligomeric behavior and dynamics.
リンク	J Mol Biol / PubMed:25636407
手法	EM (単粒子)
解像度	25.0 Å
構造データ	EMDB-6215: Yeast Rvb1 and Rvb2 proteins oligomerize as a conformationally variable dodecamer with low frequency 手法: EM (単粒子) / 解像度: 25.0 Å EMDB-6216: Yeast Rvb1 and Rvb2 proteins oligomerize as a conformationally variable dodecamer with low frequency 手法: EM (単粒子) / 解像度: 25.0 Å EMDB-6217: Yeast Rvb1 and Rvb2 proteins oligomerize as a conformationally variable dodecamer with low frequency 手法: EM (単粒子) / 解像度: 25.0 Å EMDB-6218: Yeast Rvb1 and Rvb2 proteins oligomerize as a conformationally variable dodecamer with low frequency 手法: EM (単粒子) / 解像度: 25.0 Å
由来	Saccharomyces cerevisiae (パン酵母)