Identification of human and mouse HIRA-interacting protein-5 (HIRIP5), two mammalian representatives in a family of phylogenetically conserved proteins with a role in the biogenesis of Fe/S proteins

Lorain, Stéphanie; Lécluse, Yann; Scamps, Christine; Matteï, Marie‐Geneviève; Lipinski, Marc

doi:10.1016/s0167-4781(00)00300-6

Cited by 18 publications

(26 citation statements)

References 28 publications

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“…1C Left), as expected for isoform II. These results imply that isoform I is more abundant, and are consistent with the fact that isoform I was represented by Ͼ20 ESTs in the database, whereas isoform II was reported only once (25).…”

Section: Cloning Of Human Nfusupporting

confidence: 87%

“…An initial search of DNA databases for human homologs of yeast Nfu1p identified HIRIP5 (GenBank accession no. NM 015700), which shares 39% sequence identity to Nfu1p (25). However, further analysis identified Ϸ20 human ESTs that were 90% identical to HIRIP5, but which differed in two significant ways in the 5Ј region.…”

Section: Cloning Of Human Nfumentioning

confidence: 98%

“…A human Nfu homolog, named HIRIP5, was first identified in a two-hybrid screen for proteins that interact with the transcription regulator HIRA (25). However, in this article, 5Ј RACE and PCR amplification experiments revealed additional 5Ј sequence in the complete cDNA of human nfu.…”

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confidence: 90%

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Subcellular compartmentalization of human Nfu, an iron–sulfur cluster scaffold protein, and its ability to assemble a [4Fe–4S] cluster

Tong

Jameson

Huynh

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

182

202

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Section: Cloning Of Human Nfusupporting

confidence: 87%

Section: Cloning Of Human Nfumentioning

confidence: 98%

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Subcellular compartmentalization of human Nfu, an iron–sulfur cluster scaffold protein, and its ability to assemble a [4Fe–4S] cluster

Tong

Jameson

Huynh

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

182

202

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“…The most acidic of the iron-dependently oxidized proteins selected for analysis was identified as HIRIP5, a name this protein received upon its identification in yeast as an interaction partner of a histone core binding protein [Lorain et al, 2001]. It is closely related to yeast NFU1 [Schilke et al, 1999], a gene that encodes a peptide that corresponds to the C-terminus of an iron-sulfur cluster assembly enzyme, bacterial NifU [Agar et al, 2000].…”

Section: Resultsmentioning

confidence: 99%

Numerous Proteins in Mammalian Cells Are Prone to Iron-Dependent Oxidation and Proteasomal Degradation

Drake

Bourdon²,

Wehr³

et al. 2002

Dev Neurosci

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The mechanisms that underlie iron toxicity in cells and organisms are poorly understood. Previous studies of regulation of the cytosolic iron sensor, iron-regulatory protein 2 (IRP2), indicate that iron-dependent oxidation triggers ubiquitination and proteasomal degradation of IRP2. To determine if oxidization by iron is involved in degradation of other proteins, we have used a carbonyl assay to identify oxidized proteins in lysates from RD4 cells treated with either an iron source or iron chelator. Protein lysates from iron-loaded or iron-depleted cells were resolved on two-dimensional gels and these iron manipulations were also repeated in the presence of proteasomal inhibitors. Eleven abundant proteins were identified as prone to iron-dependent oxidation and subsequent proteasomal degradation. These proteins included two putative iron-binding proteins, hNFU1 and calreticulin; two proteins involved in metabolism of hydrogen peroxide, peroxiredoxin 2 and superoxide dismutase 1; and several proteins identified in inclusions in neurodegenerative diseases, including HSP27, UCHL1, actin and tropomyosin. Our results indicate that cells can recognize and selectively eliminate iron-dependently oxidized proteins, but unlike IRP2, levels of these proteins do not significantly decrease in iron-treated cells. As iron overload is a feature of many human neurological diseases, further characterization of the process of degradation of iron-dependently oxidized proteins may yield insights into mechanisms of human disease.

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“…HIRA family member proteins are characterized by seven tryptophan-aspartic acid (WD) repeats conserved at the amino terminus, predicted to form a β-propeller structure, and the presence of nuclear localization signals. The carboxyl-terminal region of HIRA is responsible for its interaction with proteins Pax-3 (21), HIRIP, and core histones (22). Although mutational studies have identified key residues that play an important role in specifying H3.3 deposition (3,5), and more recently two key H3.3 residues were shown to be important for its recognition by DAXX protein (23,24), it is still unclear how H3.3 is targeted to transcriptionally active regions.…”

mentioning

confidence: 99%

Transcription factor EKLF (KLF1) recruitment of the histone chaperone HIRA is essential for β-globin gene expression

Soni

Pchelintsev

Adams

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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The binding of chromatin-associated proteins and incorporation of histone variants correlates with alterations in gene expression. These changes have been particularly well analyzed at the mammalian β-globin locus, where transcription factors such as erythroid Krüppel-like factor (EKLF), which is also known as Krüppel-like factor 1 (KLF1), play a coordinating role in establishing the proper chromatin structure and inducing high-level expression of adult β-globin. We had previously shown that EKLF preferentially interacts with histone H3 and that the H3.3 variant is differentially recruited to the β-globin promoter. We now find that a novel interaction between EKLF and the histone cell cycle regulation defective homolog A (HIRA) histone chaperone accounts for these effects. HIRA is not only critical for β-globin expression but is also required for activation of the erythropoietic regulators EKLF and GATA binding protein 1 (GATA1). Our results provide a mechanism by which transcription factor-directed recruitment of a generally expressed histone chaperone can lead to tissue-restricted changes in chromatin components, structure, and transcription at specific genomic sites during differentiation.

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Identification of human and mouse HIRA-interacting protein-5 (HIRIP5), two mammalian representatives in a family of phylogenetically conserved proteins with a role in the biogenesis of Fe/S proteins

Cited by 18 publications

References 28 publications

Subcellular compartmentalization of human Nfu, an iron–sulfur cluster scaffold protein, and its ability to assemble a [4Fe–4S] cluster

Subcellular compartmentalization of human Nfu, an iron–sulfur cluster scaffold protein, and its ability to assemble a [4Fe–4S] cluster

Numerous Proteins in Mammalian Cells Are Prone to Iron-Dependent Oxidation and Proteasomal Degradation

Transcription factor EKLF (KLF1) recruitment of the histone chaperone HIRA is essential for β-globin gene expression

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