Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches

Chromatin is the complex of eukaryotic DNA and proteins required for the efficient compaction of the nearly 2-meter-long human genome into a roughly 10-micron-diameter cell nucleus. The fundamental repeating unit of chromatin is the nucleosome: 147bp of DNA wrapped about an octamer of histone protei...

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Published inJournal of molecular biology Vol. 429; no. 16; pp. 2401 - 2426
Main Authors Warren, Christopher, Shechter, David
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 04.08.2017
Subjects
chromatin
Chromatin - metabolism
histone chaperone
Histone Chaperones - chemistry
Histone Chaperones - metabolism
histones
Histones - metabolism
Humans
intrinsically disordered proteins
Models, Biological
Models, Molecular
Nucleosomes - metabolism
post-translational modifications
Protein Binding
Protein Conformation
Saccharomyces cerevisiae - metabolism
Asf1
CAF-1
hSpt2
HJURP
PTM
CTAD
FACT
CABIN1
histones
NLS
IDP
IDR
UBN1
post-translational modifications
Nap1L1
Npm2
DAXX
TTLL
chromatin
histone chaperone
PML
Nap1
CTD
HDX-MS
APLF
intrinsically disordered proteins
RAPID
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Abstract Chromatin is the complex of eukaryotic DNA and proteins required for the efficient compaction of the nearly 2-meter-long human genome into a roughly 10-micron-diameter cell nucleus. The fundamental repeating unit of chromatin is the nucleosome: 147bp of DNA wrapped about an octamer of histone proteins. Nucleosomes are stable enough to organize the genome yet must be dynamically displaced and reassembled to allow access to the underlying DNA for transcription, replication, and DNA damage repair. Histone chaperones are a non-catalytic group of proteins that are central to the processes of nucleosome assembly and disassembly and thus the fluidity of the ever-changing chromatin landscape. Histone chaperones are responsible for binding the highly basic histone proteins, shielding them from non-specific interactions, facilitating their deposition onto DNA, and aiding in their eviction from DNA. Although most histone chaperones perform these common functions, recent structural studies of many different histone chaperones reveal that there are few commonalities in their folds. Importantly, sequence-based predictions show that histone chaperones are highly enriched in intrinsically disordered regions (IDRs) and acidic stretches. In this review, we focus on the molecular mechanisms underpinning histone binding, selectivity, and regulation of these highly dynamic protein regions. We highlight new evidence suggesting that IDRs are often critical for histone chaperone function and play key roles in chromatin assembly and disassembly pathways. [Display omitted] •IDRs and acidic stretches are common features among the structurally diverse histone chaperone family.•These regions are often directly involved in histone binding and regulation of chaperone function.•Recent studies have begun to shed light on both common and unique mechanisms of IDRs and acidic stretches in mediating chaperone:histone interactions.
AbstractList Chromatin is the complex of eukaryotic DNA and proteins required for the efficient compaction of the nearly two-meter long human genome into a roughly ten-micron diameter cell nucleus. The fundamental repeating unit of chromatin is the nucleosome: 147bp of DNA wrapped about an octamer of histone proteins. Nucleosomes are stable enough to organize the genome yet must be dynamically displaced and reassembled to allow access to the underlying DNA for transcription, replication, and DNA damage repair. Histone chaperones are a non-catalytic group of proteins that are central to the processes of nucleosome assembly and disassembly, and thus the fluidity of the ever-changing chromatin landscape. Histone chaperones are responsible for binding the highly basic histone proteins, shielding them from non-specific interactions, facilitating their deposition onto DNA, and aiding in their eviction from DNA. Though most histone chaperones perform these common functions, recent structural studies of many different histone chaperones reveal that there are few commonalities in their folds. Importantly, sequence-based predictions show that histone chaperones are highly enriched in intrinsically disordered regions (IDRs) and acidic stretches. In this review, we focus on the molecular mechanisms underpinning histone binding, selectivity, and regulation of these highly dynamic protein regions. We highlight new evidence suggesting that IDRs are often critical for histone chaperone function and play key roles in chromatin assembly and disassembly pathways.
Chromatin is the complex of eukaryotic DNA and proteins required for the efficient compaction of the nearly 2-meter-long human genome into a roughly 10-micron-diameter cell nucleus. The fundamental repeating unit of chromatin is the nucleosome: 147bp of DNA wrapped about an octamer of histone proteins. Nucleosomes are stable enough to organize the genome yet must be dynamically displaced and reassembled to allow access to the underlying DNA for transcription, replication, and DNA damage repair. Histone chaperones are a non-catalytic group of proteins that are central to the processes of nucleosome assembly and disassembly and thus the fluidity of the ever-changing chromatin landscape. Histone chaperones are responsible for binding the highly basic histone proteins, shielding them from non-specific interactions, facilitating their deposition onto DNA, and aiding in their eviction from DNA. Although most histone chaperones perform these common functions, recent structural studies of many different histone chaperones reveal that there are few commonalities in their folds. Importantly, sequence-based predictions show that histone chaperones are highly enriched in intrinsically disordered regions (IDRs) and acidic stretches. In this review, we focus on the molecular mechanisms underpinning histone binding, selectivity, and regulation of these highly dynamic protein regions. We highlight new evidence suggesting that IDRs are often critical for histone chaperone function and play key roles in chromatin assembly and disassembly pathways.
Chromatin is the complex of eukaryotic DNA and proteins required for the efficient compaction of the nearly 2-meter-long human genome into a roughly 10-micron-diameter cell nucleus. The fundamental repeating unit of chromatin is the nucleosome: 147bp of DNA wrapped about an octamer of histone proteins. Nucleosomes are stable enough to organize the genome yet must be dynamically displaced and reassembled to allow access to the underlying DNA for transcription, replication, and DNA damage repair. Histone chaperones are a non-catalytic group of proteins that are central to the processes of nucleosome assembly and disassembly and thus the fluidity of the ever-changing chromatin landscape. Histone chaperones are responsible for binding the highly basic histone proteins, shielding them from non-specific interactions, facilitating their deposition onto DNA, and aiding in their eviction from DNA. Although most histone chaperones perform these common functions, recent structural studies of many different histone chaperones reveal that there are few commonalities in their folds. Importantly, sequence-based predictions show that histone chaperones are highly enriched in intrinsically disordered regions (IDRs) and acidic stretches. In this review, we focus on the molecular mechanisms underpinning histone binding, selectivity, and regulation of these highly dynamic protein regions. We highlight new evidence suggesting that IDRs are often critical for histone chaperone function and play key roles in chromatin assembly and disassembly pathways. [Display omitted] •IDRs and acidic stretches are common features among the structurally diverse histone chaperone family.•These regions are often directly involved in histone binding and regulation of chaperone function.•Recent studies have begun to shed light on both common and unique mechanisms of IDRs and acidic stretches in mediating chaperone:histone interactions.
Author Shechter, David
Warren, Christopher
AuthorAffiliation Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461
AuthorAffiliation_xml – name: Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461
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  fullname: Warren, Christopher
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  givenname: David
  orcidid: 0000-0001-9388-6004
  surname: Shechter
  fullname: Shechter, David
  email: david.shechter@einstein.yu.edu
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28610839$$D View this record in MEDLINE/PubMed
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Fri Feb 23 02:36:55 EST 2024
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 16
Keywords Asf1
CAF-1
hSpt2
HJURP
PTM
CTAD
FACT
CABIN1
histones
NLS
IDP
IDR
UBN1
post-translational modifications
Nap1L1
Npm2
DAXX
TTLL
chromatin
histone chaperone
PML
Nap1
CTD
HDX-MS
APLF
intrinsically disordered proteins
RAPID
Language English
License Copyright © 2017 Elsevier Ltd. All rights reserved.
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ORCID 0000-0001-9388-6004
OpenAccessLink https://europepmc.org/articles/pmc5544577?pdf=render
PMID 28610839
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PQPubID 23479
PageCount 26
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_5544577
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PublicationTitle Journal of molecular biology
PublicationTitleAlternate J Mol Biol
PublicationYear 2017
Publisher Elsevier Ltd
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Snippet Chromatin is the complex of eukaryotic DNA and proteins required for the efficient compaction of the nearly 2-meter-long human genome into a roughly...
Chromatin is the complex of eukaryotic DNA and proteins required for the efficient compaction of the nearly two-meter long human genome into a roughly...
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SubjectTerms chromatin
Chromatin - metabolism
histone chaperone
Histone Chaperones - chemistry
Histone Chaperones - metabolism
histones
Histones - metabolism
Humans
intrinsically disordered proteins
Models, Biological
Models, Molecular
Nucleosomes - metabolism
post-translational modifications
Protein Binding
Protein Conformation
Saccharomyces cerevisiae - metabolism
Title Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches
URI https://dx.doi.org/10.1016/j.jmb.2017.06.005
https://www.ncbi.nlm.nih.gov/pubmed/28610839
https://search.proquest.com/docview/1909745161
https://pubmed.ncbi.nlm.nih.gov/PMC5544577
Volume 429
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