The replication-independent histone H3-H4 chaperones HIR, ASF1, and RTT106 co-operate to maintain promoter fidelity.

July 1, 2021 Leave a comment
RNA polymerase II initiates from low complexity sequences so cells must reliably distinguish “real” from “cryptic” promoters and maintain fidelity to the former. Further, this must be performed under a range of conditions, including those found within inactive and highly transcribed regions. Here, we used genome-scale screening to identify those factors that regulate the use of a specific cryptic promoter and how this is influenced by the degree of transcription over the element.
We show that promoter fidelity is most reliant on histone gene transactivators (Spt10, Spt21) and H3-H4 chaperones (Asf1, HIR complex) from the replication-independent deposition pathway. Mutations of Rtt106 that abrogate its interactions with H3-H4 or dsDNA permit extensive cryptic transcription comparable with replication-independent deposition factor deletions. We propose that nucleosome shielding is the primary means to maintain promoter fidelity, and histone replacement is most efficiently mediated in yeast cells by a HIR/Asf1/H3-H4/Rtt106 pathway.

Physical association of Arabidopsis hypersensitive induced reaction proteins (HIRs) with the immune receptor RPS2.

Arabidopsis RPS2 is a typical nucleotide-binding leucine-rich repeat resistance protein, which indirectly recognizes the bacterial effector protein AvrRpt2 and thereby activates effector-triggered immunity (ETI). Previously, we identified two hypersensitive induced reaction (AtHIR) proteins, AtHIR1 (At1g09840) and AtHIR2 (At3g01290), as potential RPS2 complex components.
AtHIR proteins contain the stomatin/prohibitin/flotillin/HflK/C domain (also known as the prohibitin domain or band 7 domain). In this study, we confirmed that AtHIR1 and AtHIR2 form complexes with RPS2 in Arabidopsis and Nicotiana benthamiana using a pulldown assay and fluorescence resonance energy transfer (FRET) analysis.
Arabidopsis has four HIR family genes (AtHIR1-4). All AtHIR proteins could form homo- and hetero-oligomers in vivo and were enriched in membrane microdomains of the plasma membrane. The mRNA levels of all except AtHIR4 were significantly induced by microbe-associated molecular patterns, such as the bacterial flagellin fragment flg22.
Athir2-1 and Athir3-1 mutants allowed more growth of Pto DC3000 AvrRpt2, but not Pto DC3000, indicating that these mutations reduce RPS2-mediated ETI but do not affect basal resistance to the virulent strain. Overexpression of AtHIR1 and AtHIR2 reduced growth of Pto DC3000. Taken together, the results show that the AtHIR proteins are physically associated with RPS2, are localized in membrane microdomains, and quantitatively contribute to RPS2-mediated ETI.

Separation-of-function mutation in HPC2, a member of the HIR complex in S. cerevisiae, results in derepression of the histone genes but does not confer cryptic TATA phenotypes.

The HIR complex, which is comprised of the four proteins Hir1, Hir2, Hir3 and Hpc2, was first characterized as a repressor of three of the four histone gene loci in Saccharomyces cerevisiae. Using a bioinformatical approach, previous studies have identified a region of Hpc2 that is conserved in Schizosaccharomyces pombe and humans. Using a similar approach, we identified two additional domains, CDI and CDII, of the Hpc2 protein that are conserved among yeast species related to S. cerevisiae.
The replication-independent histone H3-H4 chaperones HIR, ASF1, and RTT106 co-operate to maintain promoter fidelity.
We showed that the N terminal CDI domain (spanning amino acids 63-79) is dispensable for HIR complex assembly, but plays an essential role in the repression of the histone genes by recruiting the HIR complex to the HIR-dependent histone gene loci. The second conserved domain, CDII (spanning amino acids 452-480), is required for the stability of the Hpc2 protein itself as well as for the assembly of the HIR complex.
In addition, we report a novel separation-of-function mutation within CDI of Hpc2, which causes derepression of the histone genes but does not confer other reported hir/hpc- phenotypes (such as Spt phenotypes, heterochromatin silencing defects and repression of cryptic promoters). This is the first direct demonstration that a separation-of-function mutation exists within the HIR complex.

The Saccharomyces cerevisiae histone chaperone Rtt106 mediates the cell cycle recruitment of SWI/SNF and RSC to the HIR-dependent histone genes.

In Saccharomyces cerevisiae, three out of the four histone gene pairs (HTA1-HTB1, HHT1-HHF1, and HHT2-HHF2) are regulated by the HIR co-repressor complex. The histone chaperone Rtt106 has recently been shown to be present at these histone gene loci throughout the cell cycle in a HIR- and Asf1-dependent manner and involved in their transcriptional repression.

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Description: The HIRA protein shares sequence similarity with Hir1p and Hir2p, the two corepressors of histone gene transcription characterized in the yeast, Saccharomyces cerevisiae. The structural features of the HIRA protein suggest that it may function as part of a multiprotein complex. Several cDNAs encoding HIRA-interacting proteins, or HIRIPs, have been identified. In vitro, the protein encoded by this gene binds HIRA, as well as H2B and H3 core histones, indicating that a complex containing HIRA-HIRIP3 could function in some aspects of chromatin and histone metabolism. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

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Description: The HIRA protein shares sequence similarity with Hir1p and Hir2p, the two corepressors of histone gene transcription characterized in the yeast, Saccharomyces cerevisiae. The structural features of the HIRA protein suggest that it may function as part of a multiprotein complex. Several cDNAs encoding HIRA-interacting proteins, or HIRIPs, have been identified. In vitro, the protein encoded by this gene binds HIRA, as well as H2B and H3 core histones, indicating that a complex containing HIRA-HIRIP3 could function in some aspects of chromatin and histone metabolism. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

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Description: The HIRA protein shares sequence similarity with Hir1p and Hir2p, the two corepressors of histone gene transcription characterized in the yeast, Saccharomyces cerevisiae. The structural features of the HIRA protein suggest that it may function as part of a multiprotein complex. Several cDNAs encoding HIRA-interacting proteins, or HIRIPs, have been identified. In vitro, the protein encoded by this gene binds HIRA, as well as H2B and H3 core histones, indicating that a complex containing HIRA-HIRIP3 could function in some aspects of chromatin and histone metabolism. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

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Description: The HIRA protein shares sequence similarity with Hir1p and Hir2p, the two corepressors of histone gene transcription characterized in the yeast, Saccharomyces cerevisiae. The structural features of the HIRA protein suggest that it may function as part of a multiprotein complex. Several cDNAs encoding HIRA-interacting proteins, or HIRIPs, have been identified. In vitro, the protein encoded by this gene binds HIRA, as well as H2B and H3 core histones, indicating that a complex containing HIRA-HIRIP3 could function in some aspects of chromatin and histone metabolism. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

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Description: The HIRA protein shares sequence similarity with Hir1p and Hir2p, the two corepressors of histone gene transcription characterized in the yeast, Saccharomyces cerevisiae. The structural features of the HIRA protein suggest that it may function as part of a multiprotein complex. Several cDNAs encoding HIRA-interacting proteins, or HIRIPs, have been identified. In vitro, the protein encoded by this gene binds HIRA, as well as H2B and H3 core histones, indicating that a complex containing HIRA-HIRIP3 could function in some aspects of chromatin and histone metabolism. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

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EUR 4250

HIRIP3, ID (HIRIP3, HIRA-interacting protein 3) (MaxLight 650)
MBS6306634-01mL 0.1mL
EUR 980

HIRIP3, ID (HIRIP3, HIRA-interacting protein 3) (MaxLight 650)
MBS6306634-5x01mL 5x0.1mL
EUR 4250

HIRIP3, ID (HIRIP3, HIRA-interacting protein 3) (MaxLight 750)
MBS6306635-01mL 0.1mL
EUR 980

HIRIP3, ID (HIRIP3, HIRA-interacting protein 3) (MaxLight 750)
MBS6306635-5x01mL 5x0.1mL
EUR 4250

Hirip3 (GFP-tagged) - Mouse HIRA interacting protein 3 (Hirip3)
MG209311 10 µg Ask for price

HIRIP3 (GFP-tagged) - Human HIRA interacting protein 3 (HIRIP3)
RG200510 10 µg Ask for price

Hirip3 (untagged) - Mouse HIRA interacting protein 3 (Hirip3), (10ug)
MC219487 10 µg Ask for price

HIRIP3 Rabbit pAb
A7014 50μL
EUR 262.15

HIRIP3 Rabbit pAb
A7014-200ul 200 ul
EUR 550.8

HIRIP3 Rabbit pAb
A7014-20ul 20 ul
EUR 219.6

HIRIP3 cDNA Clone
MBS1266829-001mgPlasmid02mLGlycerolStock 0.01mgPlasmid+0.2mLGlycerol-Stock
EUR 330

HIRIP3 cDNA Clone
MBS1266829-5x001mgPlasmid5x02mLGlycerolStock 5x0.01mgPlasmid+5x0.2mLGlycerol-Stock
EUR 1430

HIRIP3 Rabbit pAb
E45R27025N 50 ul
EUR 297.75

HIRIP3 Rabbit pAb
E2507014 100ul
EUR 225
Description: Available in various conjugation types.

HIRIP3 Rabbit pAb
MBS8546513-01mL 0.1mL
EUR 305

HIRIP3 Rabbit pAb
MBS8546513-01mLAF405L 0.1mL(AF405L)
EUR 565

HIRIP3 Rabbit pAb
MBS8546513-01mLAF405S 0.1mL(AF405S)
EUR 565

HIRIP3 Rabbit pAb
MBS8546513-01mLAF610 0.1mL(AF610)
EUR 565

HIRIP3 Rabbit pAb
MBS8546513-01mLAF635 0.1mL(AF635)
EUR 565

HIRIP3, ID (HIRIP3, HIRA-interacting protein 3) (Azide free) (HRP)
MBS6306630-02mL 0.2mL
EUR 980

HIRIP3, ID (HIRIP3, HIRA-interacting protein 3) (Azide free) (HRP)
MBS6306630-5x02mL 5x0.2mL
EUR 4250

Mouse HIRIP3 siRNA
20-abx919397
  • Ask for price
  • Ask for price
  • 15 nmol
  • 30 nmol

Human HIRIP3 siRNA
20-abx919398
  • Ask for price
  • Ask for price
  • 15 nmol
  • 30 nmol

HIRIP3 siRNA (Human)
MBS8230588-15nmol 15nmol
EUR 405

HIRIP3 siRNA (Human)
MBS8230588-30nmol 30nmol
EUR 565

HIRIP3 siRNA (Human)
MBS8230588-5x30nmol 5x30nmol
EUR 2450

HIRIP3 siRNA (Mouse)
MBS8220953-15nmol 15nmol
EUR 405

HIRIP3 siRNA (Mouse)
MBS8220953-30nmol 30nmol
EUR 565

HIRIP3 siRNA (Mouse)
MBS8220953-5x30nmol 5x30nmol
EUR 2450

Hirip3 (Myc-DDK-tagged) - Mouse HIRA interacting protein 3 (Hirip3)
MR209311 10 µg Ask for price

HIRIP3 (Myc-DDK-tagged)-Human HIRA interacting protein 3 (HIRIP3)
RC200510 10 µg Ask for price

HIRIP3 cloning plasmid
CSB-CL883612HU-10ug 10ug
EUR 451.2
Description: A cloning plasmid for the HIRIP3 gene.

Hirip3 (untagged ORF) - Rat HIRA interacting protein 3 (Hirip3), (10 ug)
RN200696 10 µg Ask for price

HIRIP3 Blocking Peptide
33R-8235 100 ug
EUR 119
Description: A synthetic peptide for use as a blocking control in assays to test for specificity of HIRIP3 antibody, catalog no. 70R-2185

HIRIP3 ELISA KIT|Human
EF010125 96 Tests
EUR 826.8

HIRIP3 (Center) Rabbit pAb
E2613959 100ul
EUR 225
Description: Available in various conjugation types.

HIRIP3 (Center) Rabbit pAb
MBS8553248-01mL 0.1mL
EUR 305

HIRIP3 (Center) Rabbit pAb
MBS8553248-01mLAF405L 0.1mL(AF405L)
EUR 565

HIRIP3 (Center) Rabbit pAb
MBS8553248-01mLAF405S 0.1mL(AF405S)
EUR 565

HIRIP3 (Center) Rabbit pAb
MBS8553248-01mLAF610 0.1mL(AF610)
EUR 565

HIRIP3 (Center) Rabbit pAb
MBS8553248-01mLAF635 0.1mL(AF635)
EUR 565

Hirip3 (Myc-DDK-tagged ORF) - Rat HIRA interacting protein 3 (Hirip3), (10 ug)
RR200696 10 µg Ask for price

Mouse HIRIP3 shRNA Plasmid
20-abx982088
  • Ask for price
  • Ask for price
  • 150 µg
  • 300 µg

Human HIRIP3 shRNA Plasmid
20-abx955558
  • Ask for price
  • Ask for price
  • 150 µg
  • 300 µg

Human HIRIP3 Protein Lysate
MBS8412938-002mg 0.02mg
EUR 365

Human HIRIP3 Protein Lysate
MBS8412938-5x002mg 5x0.02mg
EUR 1410

Hirip3 (NM_172746) Mouse Recombinant Protein
E45M45538M5 20 ug
EUR 1924.54

HIRIP3 (NM_003609) Human Recombinant Protein
E45H41978M5 20 ug
EUR 785.42

HIRIP3 (NM_003609) Human Recombinant Protein
PROTQ9BW71 20ug
EUR 1249
Description: Recombinant protein of human HIRA interacting protein 3 (HIRIP3)

HIRIP3 Peptide - middle region
MBS3238764-01mg 0.1mg
EUR 180

HIRIP3 Peptide - middle region
MBS3238764-5x01mg 5x0.1mg
EUR 730

HIRIP3 (untagged) - Homo sapiens HIRA interacting protein 3 (HIRIP3), transcript variant 2
SC331200 10 µg Ask for price

Lenti ORF clone of Hirip3 (mGFP-tagged) - Mouse HIRA interacting protein 3 (Hirip3)
MR209311L4 10 µg Ask for price

HIRIP3 Recombinant Protein (Rat)
RP204605 100 ug Ask for price
The SWI/SNF and RSC chromatin remodeling complexes are both recruited to the HIR-dependent histone genes; SWI/SNF is required for their activation in S phase, whereas RSC is implicated in their repression outside of S phase. Even though their presence at the histone genes is dependent on the HIR complex, their specific recruitment has not been well characterized. In this study we focused on characterizing the role played by the histone chaperone Rtt106 in the cell cycle-dependent recruitment of SWI/SNF and RSC complexes to the histone genes.

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