التفاصيل البيبلوغرافية
| العنوان: |
The SAS-5 N-terminal domain is a tetramer, with implications for centriole assembly in C. elegans. |
| المؤلفون: |
Shimanovskay, Ekaterina, Renping Qiao, Lesigang, Johannes, Gang Dong |
| المصدر: |
Worm; Jul-Sep2013, Vol. 2 Issue 3, pe25214-1-e25214-7, 7p |
| مصطلحات موضوعية: |
MICROTUBULES, CENTRIOLES, PROTEINS, CENTROSOMES, X-ray scattering |
| مستخلص: |
The centriole is a conserved microtubule-based organelle essential for both centrosome formation and cilium biogenesis. It has a unique 9-fold symmetry and its assembly is governed by at least five component proteins (SPD-2, ZYG-1, SAS-5, SAS-6 and SAS-4), which are recruited in a hierarchical order. Recently published structural studies of the SAS-6 N-terminal domain have greatly advanced our understanding of the mechanisms of centriole assembly. However, it remains unclear how the weak interaction between the SAS-6 N-terminal head groups could drive the assembly of a closed ring-like structure, and what determines the stacking of multiple rings on top one another in centriole duplication. We recently reported that SAS-5 binds specifically to a very narrow region of the SAS-6 central coiled coil through its C-terminal domain (CTD, residues 391-404). Here, we further demonstrate by both static light scattering and small angle X-ray scattering that the SAS-5 N-terminal domain (NT D, residues 1-260) forms a tetramer. Specifically, we found that the tetramer is formed by SAS-5 residues 82-260, whereas residues 1-81 are intrinsically disordered. Taking these results together, we propose a working model for SAS-5-mediated assembly of the multi-layered central tube structure. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
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