ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli.
about
Iron and sulfur in proteins. How does the cell build Fe-S clusters, cofactors essential for life?Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster deliverySpecialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins.Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes.Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriersReconstruction and evaluation of the synthetic bacterial MEP pathway in Saccharomyces cerevisiaeTurning Escherichia coli into a Frataxin-Dependent OrganismThe DUF59 Containing Protein SufT Is Involved in the Maturation of Iron-Sulfur (FeS) Proteins during Conditions of High FeS Cofactor Demand in Staphylococcus aureusDelivery of iron-sulfur clusters to the hydrogen-oxidizing [NiFe]-hydrogenases in Escherichia coli requires the A-type carrier proteins ErpA and IscAA-type carrier protein ErpA is essential for formation of an active formate-nitrate respiratory pathway in Escherichia coli K-12.Proteomic analysis of iron acquisition, metabolic and regulatory responses of Yersinia pestis to iron starvation.Iron-sulfur cluster biosynthesis.DsrR, a novel IscA-like protein lacking iron- and Fe-S-binding functions, involved in the regulation of sulfur oxidation in Allochromatium vinosumISCA1 is essential for mitochondrial Fe4S4 biogenesis in vivo.Deep sequencing-based analysis of the anaerobic stimulon in Neisseria gonorrhoeae.Iron-binding activity of human iron-sulfur cluster assembly protein hIscA1Proteomic analysis of protein-protein interactions within the Cysteine Sulfinate Desulfinase Fe-S cluster biogenesis system.In vivo evidence for the iron-binding activity of an iron-sulfur cluster assembly protein IscA in Escherichia coli.Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes.Decreased transport restores growth of a Salmonella enterica apbC mutant on tricarballylateIscR of Rhodobacter sphaeroides functions as repressor of genes for iron-sulfur metabolism and represents a new type of iron-sulfur-binding protein.Evolution of Fe/S cluster biogenesis in the anaerobic parasite Blastocystis.A Regulatory Circuit Composed of a Transcription Factor, IscR, and a Regulatory RNA, RyhB, Controls Fe-S Cluster Delivery.Separate FeS scaffold and carrier functions for SufB₂C₂ and SufA during in vitro maturation of [2Fe2S] FdxSpectroscopic and functional characterization of iron-sulfur cluster-bound forms of Azotobacter vinelandii (Nif)IscA.Iron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesisSalmonella enterica requires ApbC function for growth on tricarballylate: evidence of functional redundancy between ApbC and IscUFe-S cluster assembly pathways in bacteria.Methylerythritol phosphate pathway of isoprenoid biosynthesis.IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions.Mechanistic aspects of carotenoid biosynthesis.Mammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20Global identification of genes affecting iron-sulfur cluster biogenesis and iron homeostasis.Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors.A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier.Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe-S cluster ligationGenome analysis of Chlamydomonas reinhardtii reveals the existence of multiple, compartmentalized iron-sulfur protein assembly machineries of different evolutionary origins.Investigating the role(s) of SufT and the domain of unknown function 59 (DUF59) in the maturation of iron-sulfur proteins.Strategies for manipulation of oxygen utilization by the electron transfer chain in microbes for metabolic engineering purposes.The human mitochondrial ISCA1, ISCA2, and IBA57 proteins are required for [4Fe-4S] protein maturation.
P2860
Q26829187-D0E6A973-435A-4186-8AE2-46A9C8251C03Q26850111-6D1C56B5-5681-4DC0-83CF-6BCD02C53879Q27931818-DC3246F3-653F-4D8B-AF41-98A07FF9072CQ27937403-54E42C4D-293B-4DAB-85DB-EE5012A1A2B8Q28475542-0F822E79-9BED-4D1C-8C3A-2DFF7AFA1CDFQ28484642-D8211D26-B024-466B-A1D9-47CA4F33A46DQ28547414-0F012F5B-93DC-4355-840A-5FFB47A81E23Q28553511-1768F414-CB52-4F51-9E7E-24E1A77C5BA9Q30318165-62453537-BD2E-4505-8C68-B06C2DCEC957Q30318269-24D61675-C82C-4A1D-A681-1107B232FB37Q33527554-83B80726-55F2-4A20-96B1-015891CC6F7DQ33685054-3FA18FA2-822D-46E6-8E0E-2E0AD7649783Q33705106-28FB082E-0FA4-42CA-AB13-762E47E04CB5Q33705545-3934F08A-DA36-44D8-B624-153FA3E3AC05Q33798568-9A2405A7-3227-4B0D-8969-AFCD768263A1Q33885897-06EEDB95-1A06-4C39-B9C0-BBF6573282CAQ34343135-CB89BC0D-ED06-4690-AA13-76413A888660Q34354270-4DE1A450-1009-49A1-AD7B-08D23380F5C5Q35286550-09C29C87-192A-4440-A876-B21D6C1C6918Q35688811-2F82985C-7624-48E6-9BA7-12185550B94AQ35733964-6E74C51F-59DE-4F43-8C3E-1026B9A9A8B6Q36068922-D36D4558-2713-41C3-83B5-F6BDA8A5E239Q36139087-84D614BB-35C1-4EB4-B68A-AD4223D72685Q36354561-8D16F316-63C3-40ED-B9BE-AB1721D01BD6Q36565932-509CED92-1A43-4CDB-8D62-C179A498D104Q36601610-FE016C37-1755-4813-8691-F85DFA9707B9Q36747310-5B7EEB1F-AB3B-43AD-BEAC-A2D9C50E85C6Q37102850-D683D77D-77E4-4B60-B82F-30BB6F76B451Q37272872-30E6F628-C53A-45FF-AD82-126C7856552AQ37419753-A36E4B90-E7C8-4044-AC9F-72E964ABFA59Q37503777-B789AFE8-0F27-4C4E-8B47-87CF5D80BFBFQ37590176-23F0D593-7F36-4D4A-BAC4-39F49A9DBB5AQ37643419-09DD4CD5-0908-47F9-B08A-850714E6E9C3Q37878385-15BBEF0E-0666-49BE-86A0-CCA6E27446FBQ38291272-FF591985-680E-439B-86A1-A1F15B7AD619Q38355137-3835A7DD-AE1C-44EC-A4FA-6A2568C92518Q38567270-CBCAAA9F-83FB-424F-818E-C7FC462969DAQ38673933-6AD6C2E6-0B5C-41D3-9C5A-D59B30FD62BCQ40472328-DFA495A8-DD36-43C3-898F-DD11B155A858Q42072342-2D43E1AA-EFBE-4F9B-916B-4A386CB314AE
P2860
ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
ErpA, an iron sulfur (Fe S) pr ...... etabolism in Escherichia coli.
@ast
ErpA, an iron sulfur (Fe S) pr ...... etabolism in Escherichia coli.
@en
type
label
ErpA, an iron sulfur (Fe S) pr ...... etabolism in Escherichia coli.
@ast
ErpA, an iron sulfur (Fe S) pr ...... etabolism in Escherichia coli.
@en
prefLabel
ErpA, an iron sulfur (Fe S) pr ...... etabolism in Escherichia coli.
@ast
ErpA, an iron sulfur (Fe S) pr ...... etabolism in Escherichia coli.
@en
P2093
P2860
P356
P1476
ErpA, an iron sulfur (Fe S) pr ...... metabolism in Escherichia coli
@en
P2093
Béatrice Py
Catherine Gerez
Joost Teixeira de Mattos
Laurent Loiseau
Marc Fontecave
Martijn Bekker
Sandrine Ollagnier-de Choudens
Yannis Sanakis
P2860
P304
13626-13631
P356
10.1073/PNAS.0705829104
P407
P577
2007-08-14T00:00:00Z