10.6084/m9.figshare.5629990
Tamiza Nanji
Tamiza
Nanji
Xu Liu
Xu
Liu
Leon H. Chew
Leon
H. Chew
Franco K. Li
Franco K.
Li
Maitree Biswas
Maitree
Biswas
Zhong-Qiu Yu
Zhong-Qiu
Yu
Shan Lu
Shan
Lu
Meng-Qiu Dong
Meng-Qiu
Dong
Li-Lin Du
Li-Lin
Du
Daniel J. Klionsky
Daniel
J. Klionsky
Calvin K. Yip
Calvin K.
Yip
Conserved and unique features of the fission yeast core Atg1 complex
Taylor & Francis Group
2017
Atg1
Atg101
Atg17
cross-linking coupled to mass spectrometry
electron microscopy (EM)
protein-protein interaction
Schizosaccharomyces pombe
ULK1
2017-11-23 11:18:44
Dataset
https://tandf.figshare.com/articles/dataset/Conserved_and_unique_features_of_the_fission_yeast_core_Atg1_complex/5629990
<p>Although the human ULK complex mediates phagophore initiation similar to the budding yeast <i>Saccharomyces cerevisiae</i> Atg1 complex, this complex contains ATG101 but not Atg29 and Atg31. Here, we analyzed the fission yeast <i>Schizosaccharomyces pombe</i> Atg1 complex, which has a subunit composition that resembles the human ULK complex. Our pairwise coprecipitation experiments showed that while the interactions between Atg1, Atg13, and Atg17 are conserved, Atg101 does not bind Atg17. Instead, Atg101 interacts with the HORMA domain of Atg13 and this enhances the stability of both proteins. We also found that <i>S. pombe</i> Atg17, the putative scaffold subunit, adopts a rod-shaped structure with no discernible curvature. Interestingly, <i>S. pombe</i> Atg17 binds <i>S. cerevisiae</i> Atg13, Atg29, and Atg31 in vitro, but it cannot complement the function of <i>S. cerevisiae</i> Atg17 in vivo. Furthermore, <i>S. pombe</i> Atg101 cannot substitute for the function of <i>S. cerevisiae</i> Atg29 and Atg31 in vivo. Collectively, our work generates new insights into the subunit organization and structural properties of an Atg101-containing Atg1/ULK complex.</p>