scholarly journals Iron–Sulfur Cluster Engineering Provides Insight into the Evolution of Substrate Specificity among Sulfonucleotide Reductases

2011 ◽  
Vol 7 (2) ◽  
pp. 306-315 ◽  
Author(s):  
Devayani P. Bhave ◽  
Jiyoung A. Hong ◽  
Rebecca L. Keller ◽  
Carsten Krebs ◽  
Kate S. Carroll
Keyword(s):  
Substrate Specificity ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Insight Into

scholarly journals Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Nicholas G. Fox ◽  
Xiaodi Yu ◽  
Xidong Feng ◽  
Henry J. Bailey ◽  
Alain Martelli ◽  
...  
Keyword(s):  
Activation Mechanism ◽  
Cluster Assembly ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Insight Into

scholarly journals Structural Alterations of the Cysteine Desulfurase IscS of Salmonella enterica Serovar Typhimurium Reveal Substrate Specificity of IscS in tRNA Thiolation

2006 ◽  
Vol 188 (8) ◽  
pp. 3052-3062 ◽  
Author(s):  
Hans K. Lundgren ◽  
Glenn R. Björk
Keyword(s):  
Substrate Specificity ◽  
Salmonella Enterica ◽  
Cluster Formation ◽  
Cysteine Desulfurase ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Serovar Typhimurium ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

ABSTRACT The cysteine desulfurase IscS in Salmonella enterica serovar Typhimurium is required for the formation of all four thiolated nucleosides in tRNA, which is thought to occur via two principally different biosynthetic pathways. The synthesis of 4-thiouridine (s4U) and 5-methylaminomethyl-2-thiouridine (mnm5s2U) occurs by a transfer of sulfur from IscS via various proteins to the target nucleoside in the tRNA, and no iron-sulfur cluster protein participates, whereas the synthesis of 2-thiocytidine (s2C) and N 6-(4-hydroxyisopentenyl)-2-methylthioadenosine (ms2io6A) is dependent on iron-sulfur cluster proteins, whose formation and maintenance depend on IscS. Accordingly, inactivation of IscS should result in decreased synthesis of all thiolated nucleosides. We selected mutants defective either in the synthesis of a thiolated nucleoside (mnm5s2U) specific for the iron-sulfur protein-independent pathway or in the synthesis of a thiolated nucleoside (ms2io6A) specific for the iron-sulfur protein-dependent pathway. Although we found altered forms of IscS that influenced the synthesis of all thiolated nucleosides, consistent with the model, we also found mutants defective in subsets of thiolated nucleosides. Alterations in the C-terminal region of IscS reduced the level of only ms2io6A, suggesting that the synthesis of this nucleoside is especially sensitive to minor aberrations in iron-sulfur cluster transfer activity. Our results suggest that IscS has an intrinsic substrate specificity in how it mediates sulfur mobilization and/or iron-sulfur cluster formation and maintenance required for thiolation of tRNA.

Structural Insight into Poplar Glutaredoxin C1 with a Bridging Iron−Sulfur Cluster at the Active Site†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (26) ◽  
pp. 7998-8008 ◽  
Author(s):  
Yingang Feng ◽  
Nan Zhong ◽  
Nicolas Rouhier ◽  
Toshiharu Hase ◽  
Masami Kusunoki ◽  
...  
Keyword(s):  
Active Site ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Structural Insight ◽  
Insight Into

scholarly journals Hsc66 Substrate Specificity Is Directed toward a Discrete Region of the Iron-Sulfur Cluster Template Protein IscU

2002 ◽  
Vol 277 (30) ◽  
pp. 27353-27359 ◽  
Author(s):  
Kevin G. Hoff ◽  
Dennis T. Ta ◽  
Tim L. Tapley ◽  
Jonathan J. Silberg ◽  
Larry E. Vickery
Keyword(s):  
Substrate Specificity ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Discrete Region ◽  
Template Protein

Two Novel Monothiol Glutaredoxins fromSaccharomyces cerevisiaeProvide Further Insight into Iron-Sulfur Cluster Binding, Oligomerization, and Enzymatic Activity of Glutaredoxins†

Biochemistry ◽  
2008 ◽  
Vol 47 (5) ◽  
pp. 1452-1463 ◽  
Author(s):  
Nikola Mesecke ◽  
Sarah Mittler ◽  
Elisabeth Eckers ◽  
Johannes M. Herrmann ◽  
Marcel Deponte
Keyword(s):  
Enzymatic Activity ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Insight Into
Sign in / Sign up

Export Citation Format

Share Document