- EMDB-20568: The axonemal doublet microtubule focusing on the I1 dynein region... -
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データベース: EMDB / ID: EMD-20568
タイトル
The axonemal doublet microtubule focusing on the I1 dynein region extracted from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas tctex2b mutant cilia
マップデータ
The I1 dynein region of the from Chlamydomonas tctex2b mutant
試料
細胞器官・細胞要素: The I1 dynein averaged from Chlamydomonas tctex2b cilia
National Institutes of Health/National Institute of General Medical Sciences
R01GM083122
米国
National Institutes of Health/National Institute of General Medical Sciences
R01GM112050
米国
引用
ジャーナル: FASEB J / 年: 2021 タイトル: Structural organization of the intermediate and light chain complex of Chlamydomonas ciliary I1 dynein. 著者: Gang Fu / Chasity Scarbrough / Kangkang Song / Nhan Phan / Maureen Wirschell / Daniela Nicastro / 要旨: Axonemal I1 dynein (dynein f) is the largest inner dynein arm in cilia and a key regulator of ciliary beating. It consists of two dynein heavy chains, and an intermediate chain/light chain (ICLC) ...Axonemal I1 dynein (dynein f) is the largest inner dynein arm in cilia and a key regulator of ciliary beating. It consists of two dynein heavy chains, and an intermediate chain/light chain (ICLC) complex. However, the structural organization of the nine ICLC subunits remains largely unknown. Here, we used biochemical and genetic approaches, and cryo-electron tomography imaging in Chlamydomonas to dissect the molecular architecture of the I1 dynein ICLC complex. Using a strain expressing SNAP-tagged IC140, tomography revealed the location of the IC140 N-terminus at the proximal apex of the ICLC structure. Mass spectrometry of a tctex2b mutant showed that TCTEX2B dynein light chain is required for the stable assembly of TCTEX1 and inner dynein arm interacting proteins IC97 and FAP120. The structural defects observed in tctex2b located these 4 subunits in the center and bottom regions of the ICLC structure, which overlaps with the location of the IC138 regulatory subcomplex, which contains IC138, IC97, FAP120, and LC7b. These results reveal the three-dimensional organization of the native ICLC complex and indicate potential protein-protein interactions that are involved in the pathway by which I1 regulates ciliary motility.