| Characteristics of the Isu1 C-terminus in relation to [2Fe-2S] cluster assembly and ISCU Myopathy. | Characteristics of the Isu1 C-terminus in relation to [2Fe-2S] cluster assembly and ISCU Myopathy.
Lewis BE, Campbell CJ, Rodrigues A, Thompson L, Pandey AK, Gallagher SN, Pain D, Dancis A, Stemmler TL. | 11/19/2022 |
| In the absence of Yfh1, Isu1 was found to exist in two forms, one mostly monomeric with limited tendency to dimerize, distinct structural features suggest that in physiological conditions the zinc-regulated abundance of monomeric vs. oligomeric Isu1 yields [Yfh1].[Isu1] complexes with different Isu1 configurations that afford unique functional properties for Fe-S cluster assembly and delivery. | Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe-S cluster assembly centers.
Galeano BK, Ranatunga W, Gakh O, Smith DY, Thompson JR, Isaya G., Free PMC Article | 07/21/2018 |
| Proteomic and metabolomic comparisons revealed that the xylose-metabolizing mutant strains exhibit altered metabolic pathways relative to the parental strain when grown in xylose. Further analyses revealed that interacting mutations in HOG1 and ISU1 unexpectedly elevated mitochondrial respiratory proteins and enabled rapid aerobic respiration of xylose and other non-fermentable carbon substrates. | Directed Evolution Reveals Unexpected Epistatic Interactions That Alter Metabolic Regulation and Enable Anaerobic Xylose Use by Saccharomyces cerevisiae.
Sato TK, Tremaine M, Parreiras LS, Hebert AS, Myers KS, Higbee AJ, Sardi M, McIlwain SJ, Ong IM, Breuer RJ, Avanasi Narasimhan R, McGee MA, Dickinson Q, La Reau A, Xie D, Tian M, Reed JL, Zhang Y, Coon JJ, Hittinger CT, Gasch AP, Landick R., Free PMC Article | 04/29/2017 |
| Isu is a substrate of the Lon-type protease and that it is protected from degradation by Nfs1, the sulfur donor for Fe-S cluster assembly, as well as by Jac1, the J-protein Hsp70 cochaperone that functions in cluster transfer from Isu. Nfs1 and Jac1 variants known to be defective in interaction with Isu were also defective in protecting Isu from degradation. | Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulation.
Ciesielski SJ, Schilke B, Marszalek J, Craig EA., Free PMC Article | 01/14/2017 |
| Studied the structure and dynamics of the yeast Isu1-Jac1 complex. | Molecular modeling of the binding modes of the iron-sulfur protein to the Jac1 co-chaperone from Saccharomyces cerevisiae by all-atom and coarse-grained approaches.
Mozolewska MA, Krupa P, Scheraga HA, Liwo A., Free PMC Article | 05/7/2016 |
| The eukaryotic forms are critical for Fe-S cluster assembly whereas prokaryotic forms are more dispensable. We found that a key to this difference is a single amino acid in the scaffold protein Isu1 at position 141. | Turning Saccharomyces cerevisiae into a Frataxin-Independent Organism.
Yoon H, Knight SA, Pandey A, Pain J, Turkarslan S, Pain D, Dancis A., Free PMC Article | 04/30/2016 |
| Fe/S cluster synthesis on Isu1 requires the ferredoxin Yah1 | Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin.
Webert H, Freibert SA, Gallo A, Heidenreich T, Linne U, Amlacher S, Hurt E, Mühlenhoff U, Banci L, Lill R. | 01/16/2016 |
| Mutual exclusivity of cluster assembly factor (Nfs1/Yfh1) and cluster transfer factor (Jac1/Ssq1) binding to Isu has functional consequences for the transition from the assembly process to the transfer process during biogenesis of FeS cluster proteins. | Overlapping binding sites of the frataxin homologue assembly factor and the heat shock protein 70 transfer factor on the Isu iron-sulfur cluster scaffold protein.
Manicki M, Majewska J, Ciesielski S, Schilke B, Blenska A, Kominek J, Marszalek J, Craig EA, Dutkiewicz R., Free PMC Article | 01/3/2015 |
| In frataxin-deleted strains expressing the bypass mutant Isu1, cell growth and iron homeostasis are restored to close to normal. | Frataxin-bypassing Isu1: characterization of the bypass activity in cells and mitochondria.
Yoon H, Knight SA, Pandey A, Pain J, Zhang Y, Pain D, Dancis A., Free PMC Article | 05/10/2014 |
| The data presented here show that the Isu1 suppressor mimics the frataxin effects on Nfs1, explaining the bypassing activity. | Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly.
Pandey A, Gordon DM, Pain J, Stemmler TL, Dancis A, Pain D., Free PMC Article | 02/22/2014 |
| Data show that mitochondrial Hsp70 chaperone Ssq1 interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from that of Isu1. | The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.
Uzarska MA, Dutkiewicz R, Freibert SA, Lill R, Mühlenhoff U., Free PMC Article | 01/18/2014 |
| Competition between Jac1 and Nfs1 for Isu binding plays an important role in transitioning the iron/Sulfur cluster biogenesis machinery. | Binding of the chaperone Jac1 protein and cysteine desulfurase Nfs1 to the iron-sulfur cluster scaffold Isu protein is mutually exclusive.
Majewska J, Ciesielski SJ, Schilke B, Kominek J, Blenska A, Delewski W, Song JY, Marszalek J, Craig EA, Dutkiewicz R., Free PMC Article | 12/7/2013 |
| Jac1:Isu1 interaction plays an indispensable role in the essential process of mitochondrial Fe-S cluster biogenesis | Interaction of J-protein co-chaperone Jac1 with Fe-S scaffold Isu is indispensable in vivo and conserved in evolution.
Ciesielski SJ, Schilke BA, Osipiuk J, Bigelow L, Mulligan R, Majewska J, Joachimiak A, Marszalek J, Craig EA, Dutkiewicz R., Free PMC Article | 07/14/2012 |
| The present paper reported that a single amino acid substitution in the mature form of Isu1 restored many deficient functions in yfh1 or frataxin-depleted yeast cells. | Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.
Yoon H, Golla R, Lesuisse E, Pain J, Donald JE, Lyver ER, Pain D, Dancis A., Free PMC Article | 02/18/2012 |
| YFH1 interacts with Isu1 through the conserved Trp-131. | Frataxin interacts with Isu1 through a conserved tryptophan in its beta-sheet.
Leidgens S, De Smet S, Foury F. | 03/22/2010 |
| The studies indicate that the Isu proteins and the iron-sulfur pathway can donate iron to Sod2p. | The interaction of mitochondrial iron with manganese superoxide dismutase.
Naranuntarat A, Jensen LT, Pazicni S, Penner-Hahn JE, Culotta VC., Free PMC Article | 01/21/2010 |
| Results are consistent with the existence of a mechanism to increase the stability of Isu, and thus its level, that is dependent on the presence of the cysteine desulfurase Nfs1. | Posttranslational regulation of the scaffold for Fe-S cluster biogenesis, Isu.
Andrew AJ, Song JY, Schilke B, Craig EA., Free PMC Article | 01/21/2010 |
| These results support the idea that the surface of the beta-sheet, adjacent to the acidic, iron binding ridge, is important for interaction of Yfh1 with the Fe-S cluster scaffold and point to a critical role for frataxin in Fe-S cluster biogenesis. | Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, Isu.
Wang T, Craig EA., Free PMC Article | 01/21/2010 |
| Ssq1p/Jac1p/Mge1p are not important for Fe/S cluster synthesis on Isu1p | The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p.
Dutkiewicz R, Marszalek J, Schilke B, Craig EA, Lill R, Mühlenhoff U. | 01/21/2010 |
| formation of a Jac1-Isu1 complex can overcome a lowered affinity of Ssq1 for Isu in vivo as well as in vitro | Compensation for a defective interaction of the hsp70 ssq1 with the mitochondrial Fe-S cluster scaffold isu.
Knieszner H, Schilke B, Dutkiewicz R, D'Silva P, Cheng S, Ohlson M, Craig EA, Marszalek J. | 01/21/2010 |
| analysis of the interaction between Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p | Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p.
Andrew AJ, Dutkiewicz R, Knieszner H, Craig EA, Marszalek J. | 01/21/2010 |