gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Cytosolic iron-sulfur protein assembly 1

Cia1, Cia1p, Ciao1
Top mentioned proteins: CIA, Histone, TBP, CAN, H4
Papers on Cia1
The Association of the Xeroderma Pigmentosum Group D DNA Helicase (XPD) with Transcription Factor IIH Is Regulated by the Cytosolic Iron-Sulfur Cluster Assembly Pathway.
New
Wohlschlegel et al., Los Angeles, United States. In J Biol Chem, Jun 2015
We recently identified a cytoplasmic Fe-S cluster assembly (CIA) targeting complex composed of MMS19, CIAO1, and FAM96B that is required for the biogenesis of extramitochondrial Fe-S proteins including XPD.
Viperin is an iron-sulfur protein that inhibits genome synthesis of tick-borne encephalitis virus via radical SAM domain activity.
Weber et al., Umeå, Sweden. In Cell Microbiol, 2014
Wt viperin was found to require ER localization for full antiviral activity and to interact with the cytosolic Fe/S protein assembly factor CIAO1. Radiolabelling in vivo revealed incorporation of (55) Fe, indicative for the presence of an Fe-S cluster.
Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and maturation of different subsets of cytosolic-nuclear iron-sulfur proteins.
Impact
Lill et al., Marburg an der Lahn, Germany. In Cell Metab, 2013
Here, we identify and characterize human CIA2A (FAM96A), CIA2B (FAM96B), and CIA1 (CIAO1) as components of the cytosolic Fe/S protein assembly (CIA) machinery.
IOP1 protein is an external component of the human cytosolic iron-sulfur cluster assembly (CIA) machinery and functions in the MMS19 protein-dependent CIA pathway.
Tanaka et al., Suita, Japan. In J Biol Chem, 2013
Here, we show that MMS19, MIP18, and CIAO1 form a tight "core" complex and that IOP1 is an "external" component of this complex.
The mammalian proteins MMS19, MIP18, and ANT2 are involved in cytoplasmic iron-sulfur cluster protein assembly.
Uringa et al., Groningen, Netherlands. In J Biol Chem, 2013
Here, we show that the mammalian nucleotide excision repair protein homolog MMS19 can simultaneously bind probable cytosolic iron-sulfur protein assembly protein CIAO1 and Fe-S proteins, confirming that MMS19 is a central protein of the CIA machinery that brings Fe-S cluster donor proteins and the receiving apoproteins into proximity.
The leaf reticulate mutant dov1 is impaired in the first step of purine metabolism.
Weber et al., Düsseldorf, Germany. In Mol Plant, 2012
dov1 is allelic to the previously characterized cia1-2 mutant that was isolated in a screen for mutants with impaired chloroplast protein import.
Inhibited PTHLH downstream leukocyte adhesion-mediated protein amino acid N-linked glycosylation coupling Notch and JAK-STAT cascade to iron-sulfur cluster assembly-induced aging network in no-tumor hepatitis/cirrhotic tissues (HBV or HCV infection) by systems-theoretical analysis.
Diao et al., Beijing, China. In Integr Biol (camb), 2012
Inhibited PTHLH downstream leukocyte adhesion-mediated protein amino acid N-linked glycosylation coupling Notch and JAK-STAT cascade to iron-sulfur cluster assembly-induced aging network included TSTA3, ALK, CIAO1, NOTCH3 in no-tumor hepatitis/cirrhotic tissues from the GEO data set using gene regulatory network inference method and our programming.
The DUF59 family gene AE7 acts in the cytosolic iron-sulfur cluster assembly pathway to maintain nuclear genome integrity in Arabidopsis.
Cui et al., Shanghai, China. In Plant Cell, 2012
AE7 is part of a protein complex with CIA1, NAR1, and MET18, which are highly conserved in eukaryotes and are involved in the biogenesis of cytosolic and nuclear Fe-S proteins.
MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism.
Impact
Boulton et al., London, United Kingdom. In Science, 2012
Here, we demonstrate that MMS19 forms a complex with the cytoplasmic Fe-S assembly (CIA) proteins CIAO1, IOP1, and MIP18.
The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer.
Martin et al., Brisbane, Australia. In Acta Crystallogr D Biol Crystallogr, 2012
The putative metal-binding site of bacterial DUF59 proteins is not conserved in Fam96a, but Fam96a interacts tightly in vitro with Ciao1, the cytosolic iron-assembly protein.
Histone chaperone Asf1 plays an essential role in maintaining genomic stability in fission yeast.
GeneRIF
Kawamukai et al., Matsue, Japan. In Plos One, 2011
Asf1 plays an essential role in maintaining genomic stability in S. pombe.
Chromatin dynamics mediated by histone modifiers and histone chaperones in postreplicative recombination.
GeneRIF
Horikoshi et al., Sendai, Japan. In Genes Cells, 2010
Data provide the framework for a postreplicative recombination mechanism controlled by histone modifiers Rtt109 and histone chaperones Cia1/Asf1 in multiple ways.
MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome segregation.
Tanaka et al., Suita, Japan. In Mol Cell, 2010
Instead, it included FAM96B (now designated MIP18), Ciao1, and ANT2.
Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B-domain or the Cac2 C terminus.
GeneRIF
Yokoyama et al., Yokohama, Japan. In J Biol Chem, 2008
crystallographic analysis of the apo-form of fission yeast Asf1/Cia1 (SpAsf1N; residues 1-161) as well as its complexes with the B-domain of the fission yeast HIRA orthologue Hip1 (Hip1B) and the C-terminal region of the Cac2 subunit of CAF-1 (Cac2C)
Structure of the yeast WD40 domain protein Cia1, a component acting late in iron-sulfur protein biogenesis.
GeneRIF
Lill et al., Frankfurt am Main, Germany. In Structure, 2007
the crystal structure of Saccharomyces cerevisiae Cia1 to 1.7 A resolution.
Structural similarity between histone chaperone Cia1p/Asf1p and DNA-binding protein NF-kappaB.
GeneRIF
Horikoshi et al., Tsukuba, Japan. In J Biochem, 2005
The crystal structure of the evolutionarily conserved domain (residues 1-169) of Cia1p (ScCia1p-DeltaC2) was determined at 2.95 A resolution
Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast.
GeneRIF
Yokoyama et al., Yokohama, Japan. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2005
X-ray diffraction analysis of the histone chaperone cia1 from fission yeast
share on facebooktweetadd +1mail to friends