scholarly journals SSR1 is a vital regulator in plant mitochondrial iron-sulfur biosynthesis

2021 ◽  
Author(s):  
Xuanjun Feng ◽  
Huiling Han ◽  
Diana Bonea ◽  
Jie Liu ◽  
Wenhan Ying ◽  
...  

AbstractThe Arabidopsis SHORT AND SWOLLEN ROOT1 (SSR1) gene encodes a mitochondrial TPR domain-containing protein and was previously reported to function in maintaining mitochondria function. In a screen for suppressors of the short-root phenotype of the loss-of-function mutant ssr1-2, two mutations, sus1 and sus2 (suppressor of ssr1-2), were isolated. sus1 and sus2 result from G87D and T55M single amino acid substitution in HSCA2 (At5g09590) and ISU1 (At4g22220), both of which are core components in iron-sulfur cluster biosynthesis pathway in mitochondria (ISC). We here demonstrated that SSR1 displayed a strong chaperone-like activity and was able to enhance the binding of HSCA2 to ISU1, an essential step for the normal operation of ISC machinery. Accordingly, the enzymatic activities of several iron-sulfur proteins, the mitochondrial membrane potential and ATP content are reduced in ssr1-2. Interestingly, SSR1 appears to exist only in plant lineages, possibly conferring adaptive advantages on plant ISC machinery to environment.

2017 ◽  
Vol 292 (40) ◽  
pp. 16578-16593 ◽  
Author(s):  
Siddharth K. Tripathi ◽  
Tao Xu ◽  
Qin Feng ◽  
Bharathi Avula ◽  
Xiaomin Shi ◽  
...  

2008 ◽  
Vol 36 (6) ◽  
pp. 1112-1119 ◽  
Author(s):  
Sibali Bandyopadhyay ◽  
Kala Chandramouli ◽  
Michael K. Johnson

Iron–sulfur (Fe–S) clusters are present in more than 200 different types of enzymes or proteins and constitute one of the most ancient, ubiquitous and structurally diverse classes of biological prosthetic groups. Hence the process of Fe–S cluster biosynthesis is essential to almost all forms of life and is remarkably conserved in prokaryotic and eukaryotic organisms. Three distinct types of Fe–S cluster assembly machinery have been established in bacteria, termed the NIF, ISC and SUF systems, and, in each case, the overall mechanism involves cysteine desulfurase-mediated assembly of transient clusters on scaffold proteins and subsequent transfer of pre-formed clusters to apo proteins. A molecular level understanding of the complex processes of Fe–S cluster assembly and transfer is now beginning to emerge from the combination of in vivo and in vitro approaches. The present review highlights recent developments in understanding the mechanism of Fe–S cluster assembly and transfer involving the ubiquitous U-type scaffold proteins and the potential roles of accessory proteins such as Nfu proteins and monothiol glutaredoxins in the assembly, storage or transfer of Fe–S clusters.


2020 ◽  
Author(s):  
Sakiko Sato ◽  
Yumeka Matsushima ◽  
Miaki Kanazawa ◽  
Naoyuki Tanaka ◽  
Takashi Fujishiro ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document