scholarly journals Author response: De novo centriole formation in human cells is error-prone and does not require SAS-6 self-assembly

2015 ◽  
Author(s):  
Won-Jing Wang ◽  
Devrim Acehan ◽  
Chien-Han Kao ◽  
Wann-Neng Jane ◽  
Kunihiro Uryu ◽  
...  
eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Won-Jing Wang ◽  
Devrim Acehan ◽  
Chien-Han Kao ◽  
Wann-Neng Jane ◽  
Kunihiro Uryu ◽  
...  

Vertebrate centrioles normally propagate through duplication, but in the absence of preexisting centrioles, de novo synthesis can occur. Consistently, centriole formation is thought to strictly rely on self-assembly, involving self-oligomerization of the centriolar protein SAS-6. Here, through reconstitution of de novo synthesis in human cells, we surprisingly found that normal looking centrioles capable of duplication and ciliation can arise in the absence of SAS-6 self-oligomerization. Moreover, whereas canonically duplicated centrioles always form correctly, de novo centrioles are prone to structural errors, even in the presence of SAS-6 self-oligomerization. These results indicate that centriole biogenesis does not strictly depend on SAS-6 self-assembly, and may require preexisting centrioles to ensure structural accuracy, fundamentally deviating from the current paradigm.


2020 ◽  
Author(s):  
Li Yang ◽  
Cuiping You ◽  
Shiyan Qiu ◽  
Xiaofan Yang ◽  
Yufen Li ◽  
...  
Keyword(s):  
De Novo ◽  

2020 ◽  
Author(s):  
Keerthana Gnanapradeepan ◽  
Julia I-Ju Leu ◽  
Subhasree Basu ◽  
Thibaut Barnoud ◽  
Madeline Good ◽  
...  

2021 ◽  
Author(s):  
Jitendra Sahu ◽  
Shahbaz Lone ◽  
Kalyan Sadhu

Abstract The key steps for seed mediated growth of noble metal nanoparticles involve primary and secondary nucleation, which depends upon the energy barrier and ligand supersaturation standards of the medium. Herein we report the unique case of methionine (Met) controlled growth reaction, which rather proceeds via impeding secondary nucleation in presence of citrate stabilized gold nanoparticle (AuNP). The interaction between freshly generated Au+ and thioether group of Met in the medium restricts the secondary nucleation process involving further Au+ reduction. This incomplete conversion of Au+ results in a significant enhancement of the zeta (ζ) potential even at low concentration of Met. Furthermore, the aurophilic interaction of Au+ controls the self-assembly process of the in situ generated emissive nucleated particles. Nucleation of primary particles on seed surface, their segregation and time dependent conversion to larger particles within self-assembly confirm the nonclassical growth, which has further been explored with Met containing bio-inspired peptides.


2017 ◽  
Author(s):  
Meng Amy Li ◽  
Paulo P Amaral ◽  
Priscilla Cheung ◽  
Jan H Bergmann ◽  
Masaki Kinoshita ◽  
...  

2003 ◽  
Vol 14 (12) ◽  
pp. 5011-5018 ◽  
Author(s):  
Sapna Puri ◽  
Adam D. Linstedt

It is unclear whether the mammalian Golgi apparatus can form de novo from the ER or whether it requires a preassembled Golgi matrix. As a test, we assayed Golgi reassembly after forced redistribution of Golgi matrix proteins into the ER. Two conditions were used. In one, ER redistribution was achieved using a combination of brefeldin A (BFA) to cause Golgi collapse and H89 to block ER export. Unlike brefeldin A alone, which leaves matrix proteins in relatively large remnant structures outside the ER, the addition of H89 to BFA-treated cells caused ER accumulation of all Golgi markers tested. In the other, clofibrate treatment induced ER redistribution of matrix and nonmatrix proteins. Significantly, Golgi reassembly after either treatment was robust, implying that the Golgi has the capacity to form de novo from the ER. Furthermore, matrix proteins reemerged from the ER with faster ER exit rates. This, together with the sensitivity of BFA remnants to ER export blockade, suggests that presence of matrix proteins in BFA remnants is due to cycling via the ER and preferential ER export rather than their stable assembly in a matrix outside the ER. In summary, the Golgi apparatus appears capable of efficient self-assembly.


2015 ◽  
Vol 17 (46) ◽  
pp. 31055-31060 ◽  
Author(s):  
Emiliana De Santis ◽  
Valeria Castelletto ◽  
Maxim G. Ryadnov

A de novo self-assembly topology for engineering protein nanostructures under morphological control is reported.


2020 ◽  
Author(s):  
Pedro Fraiman ◽  
João Paulo Maia‐de‐Oliveira ◽  
Manuel Moreira‐Neto ◽  
Clecio Godeiro‐Junior

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