Nucleosome

A nucleosome is t he basic st ruct ural unit of DNA packaging in eukaryot es. The st ruct ure of a
nucleosome consist s of a segment of DNA wound around eight hist one prot eins[1] and resembles
t hread wrapped around a spool. The nucleosome is t he fundament al subunit of chromat in. Each
nucleosome is composed of a lit t le less t han t wo t urns of DNA wrapped around a set of eight
prot eins called hist ones, which are known as a hist one oct amer. Each hist one oct amer is
composed of t wo copies each of t he hist one prot eins H2A, H2B, H3, and H4.
Basic units of chromatin structure

DNA must be compact ed int o nucleosomes t o fit wit hin t he cell nucleus.[2] In addit ion t o
nucleosome wrapping, eukaryot ic chromat in is furt her compact ed by being folded int o a series
of more complex st ruct ures, event ually forming a chromosome. Each human cell cont ains about
30 million nucleosomes.[3]

Nucleosomes are t hought t o carry epigenet ically inherit ed informat ion in t he form of covalent
modificat ions of t heir core hist ones. Nucleosome posit ions in t he genome are not random, and it
is import ant t o know where each nucleosome is locat ed because t his det ermines t he
accessibilit y of t he DNA t o regulat ory prot eins.[4]

Nucleosomes were first observed as part icles in t he elect ron microscope by Don and Ada Olins
in 1974,[5] and t heir exist ence and st ruct ure (as hist one oct amers surrounded by approximat ely
200 base pairs of DNA) were proposed by Roger Kornberg.[6][7] The role of t he nucleosome as a
general gene repressor was demonst rat ed by Lorch et al. in vit ro,[8] and by Han and Grunst ein in
vivo in 1987 and 1988, respect ively.[9]

The nucleosome core part icle consist s of approximat ely 146 base pairs (bp) of DNA[10] wrapped
in 1.67 left -handed superhelical t urns around a hist one oct amer, consist ing of 2 copies each of
t he core hist ones H2A, H2B, H3, and H4.[11] Core part icles are connect ed by st ret ches of linker
DNA, which can be up t o about 80 bp long. Technically, a nucleosome is defined as t he core
part icle plus one of t hese linker regions; however t he word is oft en synonymous wit h t he core
part icle.[12] Genome-wide nucleosome posit ioning maps are now available for many model
organisms including mouse liver and brain.[13]

Linker hist ones such as H1 and it s isoforms are involved in chromat in compact ion and sit at t he
base of t he nucleosome near t he DNA ent ry and exit binding t o t he linker region of t he DNA.[14]
Non-condensed nucleosomes wit hout t he linker hist one resemble "beads on a st ring of DNA"
under an elect ron microscope.[15]

In cont rast t o most eukaryot ic cells, mat ure sperm cells largely use prot amines t o package t heir
genomic DNA, most likely t o achieve an even higher packaging rat io.[16] Hist one equivalent s and a
simplified chromat in st ruct ure have also been found in Archaea,[17] suggest ing t hat eukaryot es
are not t he only organisms t hat use nucleosomes.

Structure

Structure of the core particle

The crystal structure of the nucleosome core particle consisting of H2A , H2B , H3 and H4 core histones, and DNA. The
view is from the top through the superhelical axis.

Overview

Pioneering st ruct ural st udies in t he 1980s by Aaron Klug's group provided t he first evidence t hat
an oct amer of hist one prot eins wraps DNA around it self in about 1.7 t urns of a left -handed
superhelix.[18] In 1997 t he first near at omic resolut ion cryst al st ruct ure of t he nucleosome was
solved by t he Richmond group, showing t he most import ant det ails of t he part icle. The human
alpha sat ellit e palindromic DNA crit ical t o achieving t he 1997 nucleosome cryst al st ruct ure was
developed by t he Bunick group at Oak Ridge Nat ional Laborat ory in Tennessee.[19][20][21][22][23]
The st ruct ures of over 20 different nucleosome core part icles have been solved t o dat e,[24]
including t hose cont aining hist one variant s and hist ones from different species. The st ruct ure of
t he nucleosome core part icle is remarkably conserved, and even a change of over 100 residues
bet ween frog and yeast hist ones result s in elect ron densit y maps wit h an overall root mean
square deviat ion of only 1.6Å.[25]

The nucleosome core particle (NCP)

The nucleosome core part icle (shown in t he figure) consist s of about 146 base pair of DNA[10]
wrapped in 1.67 left -handed superhelical t urns around t he hist one oct amer, consist ing of 2
copies each of t he core hist ones H2A, H2B, H3, and H4. Adjacent nucleosomes are joined by a
st ret ch of free DNA t ermed linker DNA (which varies from 10 - 80 bp in lengt h depending on
species and t issue t ype [17]).The whole st ruct ure generat es a cylinder of diamet er 11 nm and a
height of 5.5 nm.

Apoptotic DNA laddering. Digested chromatin is in the first lane; the second contains DNA standard to compare lengths.

Scheme of nucleosome organization.[26]

The crystal structure of the nucleosome core particle (PDB: 1EQZ (https://www.rcsb.org/structure/1EQZ) [27][28]
​ )

Nucleosome core part icles are observed when chromat in in int erphase is t reat ed t o cause t he
chromat in t o unfold part ially. The result ing image, via an elect ron microscope, is "beads on a
st ring". The st ring is t he DNA, while each bead in t he nucleosome is a core part icle. The
nucleosome core part icle is composed of DNA and hist one prot eins.[29]

Part ial DNAse digest ion of chromat in reveals it s nucleosome st ruct ure. Because DNA port ions
of nucleosome core part icles are less accessible for DNAse t han linking sect ions, DNA get s
digest ed int o fragment s of lengt hs equal t o mult iplicit y of dist ance bet ween nucleosomes (180,
360, 540 base pairs et c.). Hence a very charact erist ic pat t ern similar t o a ladder is visible during
gel elect rophoresis of t hat DNA.[26] Such digest ion can occur also under nat ural condit ions during
apopt osis ("cell suicide" or programmed cell deat h), because aut odest ruct ion of DNA t ypically is
it s role.

Prot ein int eract ions wit hin t he nucleosome

The core hist one prot eins cont ains a charact erist ic st ruct ural mot if t ermed t he "hist one fold",
which consist s of t hree alpha-helices (α1-3) separat ed by t wo loops (L1-2). In solut ion, t he
hist ones form H2A-H2B het erodimers and H3-H4 het erot et ramers. Hist ones dimerise about t heir
long α2 helices in an ant i-parallel orient at ion, and, in t he case of H3 and H4, t wo such dimers form
a 4-helix bundle st abilised by ext ensive H3-H3' int eract ion. The H2A/H2B dimer binds ont o t he
H3/H4 t et ramer due t o int eract ions bet ween H4 and H2B, which include t he format ion of a
hydrophobic clust er.[11] The hist one oct amer is formed by a cent ral H3/H4 t et ramer sandwiched
bet ween t wo H2A/H2B dimers. Due t o t he highly basic charge of all four core hist ones, t he
hist one oct amer is st able only in t he presence of DNA or very high salt concent rat ions.

Hist one - DNA int eract ions

The nucleosome cont ains over 120 direct prot ein-DNA int eract ions and several hundred wat er-
mediat ed ones.[30] Direct prot ein - DNA int eract ions are not spread evenly about t he oct amer
surface but rat her locat ed at discret e sit es. These are due t o t he format ion of t wo t ypes of
DNA binding sit es wit hin t he oct amer; t he α1α1 sit e, which uses t he α1 helix from t wo adjacent
hist ones, and t he L1L2 sit e formed by t he L1 and L2 loops. Salt links and hydrogen bonding
bet ween bot h side-chain basic and hydroxyl groups and main-chain amides wit h t he DNA
backbone phosphat es form t he bulk of int eract ions wit h t he DNA. This is import ant , given t hat
t he ubiquit ous dist ribut ion of nucleosomes along genomes requires it t o be a non-sequence-
specific DNA-binding fact or. Alt hough nucleosomes t end t o prefer some DNA sequences over
ot hers,[31] t hey are capable of binding pract ically t o any sequence, which is t hought t o be due t o
t he flexibilit y in t he format ion of t hese wat er-mediat ed int eract ions. In addit ion, non-polar
int eract ions are made bet ween prot ein side-chains and t he deoxyribose groups, and an arginine
side-chain int ercalat es int o t he DNA minor groove at all 14 sit es where it faces t he oct amer
surface.
The dist ribut ion and st rengt h of DNA-binding sit es about t he oct amer surface dist ort s
t he DNA wit hin t he nucleosome core. The DNA is non-uniformly bent and also cont ains t wist
defect s. The t wist of free B-form DNA in solut ion is 10.5 bp per t urn. However, t he overall t wist
of nucleosomal DNA is only 10.2 bp per t urn, varying from a value of 9.4 t o 10.9 bp per t urn.

Histone tail domains

The hist one t ail ext ensions const it ut e up t o 30% by mass of hist ones, but are not visible in t he
cryst al st ruct ures of nucleosomes due t o t heir high int rinsic flexibilit y, and have been t hought t o
be largely unst ruct ured.[32] The N-t erminal t ails of hist ones H3 and H2B pass t hrough a channel
formed by t he minor grooves of t he t wo DNA st rands, prot ruding from t he DNA every 20 bp. The
N-t erminal t ail of hist one H4, on t he ot her hand, has a region of highly basic amino acids (16-25),
which, in t he cryst al st ruct ure, forms an int eract ion wit h t he highly acidic surface region of a
H2A-H2B dimer of anot her nucleosome, being pot ent ially relevant for t he higher-order st ruct ure
of nucleosomes. This int eract ion is t hought t o occur under physiological condit ions also, and
suggest s t hat acet ylat ion of t he H4 t ail dist ort s t he higher-order st ruct ure of chromat in.

Higher order structure

The current chromatin compaction model.

The organizat ion of t he DNA t hat is achieved by t he nucleosome cannot fully explain t he
packaging of DNA observed in t he cell nucleus. Furt her compact ion of chromat in int o t he cell
nucleus is necessary, but it is not yet well underst ood. The current underst anding[24] is t hat
repeat ing nucleosomes wit h int ervening "linker" DNA form a 10-nm-fiber, described as "beads on a
st ring", and have a packing rat io of about five t o t en.[17] A chain of nucleosomes can be arranged
in a 30 nm fiber, a compact ed st ruct ure wit h a packing rat io of ~50[17] and whose format ion is
dependent on t he presence of t he H1 hist one.

A cryst al st ruct ure of a t et ranucleosome has been present ed and used t o build up a proposed
st ruct ure of t he 30 nm fiber as a t wo-st art helix.[33]
There is st ill a cert ain amount of cont ent ion
regarding t his model, as it is incompat ible wit h recent elect ron microscopy dat a.[34] Beyond t his,
t he st ruct ure of chromat in is poorly underst ood, but it is classically suggest ed t hat t he 30 nm
fiber is arranged int o loops along a cent ral prot ein scaffold t o form t ranscript ionally act ive
euchromat in. Furt her compact ion leads t o t ranscript ionally inact ive het erochromat in.

Dynamics

Alt hough t he nucleosome is a very st able prot ein-DNA complex, it is not st at ic and has been
shown t o undergo a number of different st ruct ural re-arrangement s including nucleosome sliding
and DNA sit e exposure. Depending on t he cont ext , nucleosomes can inhibit or facilit at e
t ranscript ion fact or binding. Nucleosome posit ions are cont rolled by t hree major cont ribut ions:
First , t he int rinsic binding affinit y of t he hist one oct amer depends on t he DNA sequence. Second,
t he nucleosome can be displaced or recruit ed by t he compet it ive or cooperat ive binding of ot her
prot ein fact ors. Third, t he nucleosome may be act ively t ranslocat ed by ATP-dependent
remodeling complexes.[35]
Nucleosome sliding

Work performed in t he Bradbury laborat ory showed t hat nucleosomes reconst it ut ed ont o t he 5S
DNA posit ioning sequence were able t o reposit ion t hemselves t ranslat ionally ont o adjacent
sequences when incubat ed t hermally.[36] Lat er work showed t hat t his reposit ioning did not
require disrupt ion of t he hist one oct amer but was consist ent wit h nucleosomes being able t o
"slide" along t he DNA in cis. In 2008, it was furt her revealed t hat CTCF binding sit es act as
nucleosome posit ioning anchors so t hat , when used t o align various genomic signals, mult iple
flanking nucleosomes can be readily ident ified.[37] Alt hough nucleosomes are int rinsically mobile,
eukaryot es have evolved a large family of ATP-dependent chromat in remodelling enzymes t o
alt er chromat in st ruct ure, many of which do so via nucleosome sliding. In 2012, Beena Pillai's
laborat ory has demonst rat ed t hat nucleosome sliding is one of t he possible mechanism for large
scale t issue specific expression of genes. The work shows t hat t he t ranscript ion st art sit e for
genes expressed in a part icular t issue, are nucleosome deplet ed while, t he same set of genes in
ot her t issue where t hey are not expressed, are nucleosome bound.[13]

DNA site exposure

Work from t he Widom laborat ory has shown t hat nucleosomal DNA is in equilibrium bet ween a
wrapped and unwrapped st at e. Measurement s of t hese rat es using t ime-resolved FRET revealed
t hat DNA wit hin t he nucleosome remains fully wrapped for only 250 ms before it is unwrapped
for 10-50 ms and t hen rapidly rewrapped.[38] This implies t hat DNA does not need t o be act ively
dissociat ed from t he nucleosome but t hat t here is a significant fract ion of t ime during which it is
fully accessible. Indeed, t his can be ext ended t o t he observat ion t hat int roducing a DNA-binding
sequence wit hin t he nucleosome increases t he accessibilit y of adjacent regions of DNA when
bound.[39] This propensit y for DNA wit hin t he nucleosome t o "breat he" has import ant funct ional
consequences for all DNA-binding prot eins t hat operat e in a chromat in environment .[38] In
part icular, t he dynamic breat hing of nucleosomes plays an import ant role in rest rict ing t he
advancement of RNA polymerase II during t ranscript ion elongat ion.[40]

Nucleosome free region

Promot ers of act ive genes have nucleosome free regions (NFR). This allows for promot er DNA
accessibilit y t o various prot eins, such as t ranscript ion fact ors. Nucleosome free region t ypically
spans for 200 nucleot ides in S. cerevisae[41] Well-posit ioned nucleosomes form boundaries of
NFR. These nucleosomes are called +1-nucleosome and −1-nucleosome and are locat ed at
canonical dist ances downst ream and upst ream, respect ively, from t ranscript ion st art sit e.[42] +1-
nucleosome and several downst ream nucleosomes also t end t o incorporat e H2A.Z hist one
variant .[42]

Modulating nucleosome structure

Eukaryot ic genomes are ubiquit ously associat ed int o chromat in; however, cells must spat ially and
t emporally regulat e specific loci independent ly of bulk chromat in. In order t o achieve t he high
level of cont rol required t o co-ordinat e nuclear processes such as DNA replicat ion, repair, and
t ranscript ion, cells have developed a variet y of means t o locally and specifically modulat e
chromat in st ruct ure and funct ion. This can involve covalent modificat ion of hist ones, t he
incorporat ion of hist one variant s, and non-covalent remodelling by ATP-dependent remodeling
enzymes.

Histone post-translational modifications

Histone tails and their function in chromatin formation

Since t hey were discovered in t he mid-1960s, hist one modificat ions have been predict ed t o
affect t ranscript ion.[43] The fact t hat most of t he early post -t ranslat ional modificat ions found
were concent rat ed wit hin t he t ail ext ensions t hat prot rude from t he nucleosome core lead t o
t wo main t heories regarding t he mechanism of hist one modificat ion. The first of t he t heories
suggest ed t hat t hey may affect elect rost at ic int eract ions bet ween t he hist one t ails and DNA
t o "loosen" chromat in st ruct ure. Lat er it was proposed t hat combinat ions of t hese modificat ions
may creat e binding epit opes wit h which t o recruit ot her prot eins.[44] Recent ly, given t hat more
modificat ions have been found in t he st ruct ured regions of hist ones, it has been put forward t hat
t hese modificat ions may affect hist one-DNA[45] and hist one-hist one [46] int eract ions wit hin t he
nucleosome core. Modificat ions (such as acet ylat ion or phosphorylat ion) t hat lower t he charge
of t he globular hist one core are predict ed t o "loosen" core-DNA associat ion; t he st rengt h of t he
effect depends on locat ion of t he modificat ion wit hin t he core.[47]
Some modificat ions have
been shown t o be correlat ed wit h gene silencing; ot hers seem t o be correlat ed wit h gene
act ivat ion. Common modificat ions include acet ylat ion, met hylat ion, or ubiquit inat ion of lysine;
met hylat ion of arginine; and phosphorylat ion of serine. The informat ion st ored in t his way is
considered epigenet ic, since it is not encoded in t he DNA but is st ill inherit ed t o daught er cells.
The maint enance of a repressed or act ivat ed st at us of a gene is oft en necessary for cellular
different iat ion.[17]

Histone variants

Alt hough hist ones are remarkably conserved t hroughout evolut ion, several variant forms have
been ident ified. This diversificat ion of hist one funct ion is rest rict ed t o H2A and H3, wit h H2B and
H4 being most ly invariant . H2A can be replaced by H2AZ (which leads t o reduced nucleosome
st abilit y) or H2AX (which is associat ed wit h DNA repair and T cell different iat ion), whereas t he
inact ive X chromosomes in mammals are enriched in macroH2A. H3 can be replaced by H3.3
(which correlat es wit h act ivat e genes and regulat ory element s) and in cent romeres H3 is
replaced by CENPA.[17]

ATP-dependent nucleosome remodeling

A number of dist inct react ions are associat ed wit h t he t erm ATP-dependent chromat in
remodeling. Remodeling enzymes have been shown t o slide nucleosomes along DNA,[48] disrupt
hist one-DNA cont act s t o t he ext ent of dest abilizing t he H2A/H2B dimer[49][50] and t o generat e
negat ive superhelical t orsion in DNA and chromat in.[51] Recent ly, t he Swr1 remodeling enzyme
has been shown t o int roduce t he variant hist one H2A.Z int o nucleosomes.[52] At present , it is not
clear if all of t hese represent dist inct react ions or merely alt ernat ive out comes of a common
mechanism. What is shared bet ween all, and indeed t he hallmark of ATP-dependent chromat in
remodeling, is t hat t hey all result in alt ered DNA accessibilit y.

St udies looking at gene act ivat ion in vivo[53] and, more ast onishingly, remodeling in vitro[54] have
revealed t hat chromat in remodeling event s and t ranscript ion-fact or binding are cyclical and
periodic in nat ure. While t he consequences of t his for t he react ion mechanism of chromat in
remodeling are not known, t he dynamic nat ure of t he syst em may allow it t o respond fast er t o
ext ernal st imuli. A recent st udy indicat es t hat nucleosome posit ions change significant ly during
mouse embryonic st em cell development , and t hese changes are relat ed t o binding of
development al t ranscript ion fact ors.[55]

Dynamic nucleosome remodelling across the Yeast genome

St udies in 2007 have cat alogued nucleosome posit ions in yeast and shown t hat nucleosomes are
deplet ed in promot er regions and origins of replicat ion.[56][57][58]
About 80% of t he yeast genome
appears t o be covered by nucleosomes[59] and t he pat t ern of nucleosome posit ioning clearly
relat es t o DNA regions t hat regulat e t ranscript ion, regions t hat are t ranscribed and regions t hat
init iat e DNA replicat ion.[60] Most recent ly, a new st udy examined dynamic changes in nucleosome
reposit ioning during a global t ranscript ional reprogramming event t o elucidat e t he effect s on
nucleosome displacement during genome-wide t ranscript ional changes in yeast (Saccharomyces
cerevisiae).[61] The result s suggest ed t hat nucleosomes t hat were localized t o promot er regions
are displaced in response t o st ress (like heat shock). In addit ion, t he removal of nucleosomes
usually corresponded t o t ranscript ional act ivat ion and t he replacement of nucleosomes usually
corresponded t o t ranscript ional repression, presumably because t ranscript ion fact or binding
sit es became more or less accessible, respect ively. In general, only one or t wo nucleosomes
were reposit ioned at t he promot er t o effect t hese t ranscript ional changes. However, even in
chromosomal regions t hat were not associat ed wit h t ranscript ional changes, nucleosome
reposit ioning was observed, suggest ing t hat t he covering and uncovering of t ranscript ional DNA
does not necessarily produce a t ranscript ional event . Aft er t ranscript ion, t he rDNA region has t o
prot ect ed from any damage, it suggest ed HMGB prot eins play a major role in prot ect ing t he
nucleosome free region.[62][63]

Nucleosome assembly in vitro

Diagram of nucleosome assembly.

Nucleosomes can be assembled in vitro by eit her using purified nat ive or recombinant
hist ones.[64][65] One st andard t echnique of loading t he DNA around t he hist ones involves t he use
of salt dialysis. A react ion consist ing of t he hist one oct amers and a naked DNA t emplat e can be
incubat ed t oget her at a salt concent rat ion of 2 M. By st eadily decreasing t he salt concent rat ion,
t he DNA will equilibrat e t o a posit ion where it is wrapped around t he hist one oct amers, forming
nucleosomes. In appropriat e condit ions, t his reconst it ut ion process allows for t he nucleosome
posit ioning affinit y of a given sequence t o be mapped experiment ally.[66]

Disulfide crosslinked nucleosome core particles

A recent advance in t he product ion of nucleosome core part icles wit h enhanced st abilit y
involves sit e-specific disulfide crosslinks.[67] Two different crosslinks can be int roduced int o t he
nucleosome core part icle. A first one crosslinks t he t wo copies of H2A via an int roduced
cyst eine (N38C) result ing in hist one oct amer which is st able against H2A/H2B dimer loss during
nucleosome reconst it ut ion. A second crosslink can be int roduced bet ween t he H3 N-t erminal
hist one t ail and t he nucleosome DNA ends via an incorporat ed convert ible nucleot ide.[68] The
DNA-hist one oct amer crosslink st abilizes t he nucleosome core part icle against DNA dissociat ion
at very low part icle concent rat ions and at elevat ed salt concent rat ions.

Nucleosome assembly in vivo

Steps in nucleosome assembly

Nucleosomes are t he basic packing unit of DNA built from hist one prot eins around which DNA is
coiled. They serve as a scaffold for format ion of higher order chromat in st ruct ure as well as for
a layer of regulat ory cont rol of gene expression. Nucleosomes are quickly assembled ont o newly
synt hesized DNA behind t he replicat ion fork.

H3 and H4

Hist ones H3 and H4 from disassembled old nucleosomes are kept in t he vicinit y and randomly
dist ribut ed on t he newly synt hesized DNA.[69] They are assembled by t he chromat in assembly
fact or-1 (CAF-1) complex, which consist s of t hree subunit s (p150, p60, and p48).[70] Newly
synt hesized H3 and H4 are assembled by t he replicat ion coupling assembly fact or (RCAF). RCAF
cont ains t he subunit Asf1, which binds t o newly synt hesized H3 and H4 prot eins.[71] The old H3
and H4 prot eins ret ain t heir chemical modificat ions which cont ribut es t o t he passing down of t he
epigenet ic signat ure. The newly synt hesized H3 and H4 prot eins are gradually acet ylat ed at
different lysine residues as part of t he chromat in mat urat ion process.[72] It is also t hought t hat
t he old H3 and H4 prot eins in t he new nucleosomes recruit hist one modifying enzymes t hat mark
t he new hist ones, cont ribut ing t o epigenet ic memory.

H2A and H2B

In cont rast t o old H3 and H4, t he old H2A and H2B hist one prot eins are released and degraded;
t herefore, newly assembled H2A and H2B prot eins are incorporat ed int o new nucleosomes.[73]
H2A and H2B are assembled int o dimers which are t hen loaded ont o nucleosomes by t he
nucleosome assembly prot ein-1 (NAP-1) which also assist s wit h nucleosome sliding.[74] The
nucleosomes are also spaced by ATP-dependent nucleosome-remodeling complexes cont aining
enzymes such as Isw1 Ino80, and Chd1, and subsequent ly assembled int o higher order
st ruct ure.[75][76]

Gallery
The cryst al st ruct ure of t he nucleosome core part icle (PDB: 1EQZ (ht t ps://www.rcsb.org/st ruct
ure/1EQZ) [27][28]
​ ) - different views showing det ails of hist one folding and organizat ion. Hist ones
H2A, H2B, H3, H4 and DNA are coloured.
See also

Chromomere

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External links

MBInfo - What are nucleosomes (ht t p://www.mechanobio.info/t opics/synt hesis/go-0006323#

01_ go-0006323)

Nucleosomes on t he Richmond Lab websit e (ht t ps://www.et hz.ch/cont ent /specialint erest /bi
ol/inst it ut e-molecular-biology-biophysics/richmond-group/en.ht ml)

Proteopedia Nucleosomes (http://www.proteopedia.org/wiki/index.php/Nucleosomes)

Nucleosome at t he PDB (ht t ps://web.archive.org/web/20090111044350/ht t p://pdb.rcsb.org/

pdb/st at ic.do?p=educat ion_ discussion%2Fmolecule_ of_ t he_ mont h%2Fpdb7_ 1.ht ml)

Dynamic Remodeling of Individual Nucleosomes Across a Eukaryot ic Genome in Response t o

Transcript ional Pert urbat ion (ht t ps://web.archive.org/web/20090803083240/ht t p://www.scive
e.t v/node/5532)

Nucleosome posit ioning dat a and t ools online (annot at ed list , const ant ly updat ed) (ht t ps://ge
neregulat ion.org/nucleosome-posit ioning-dat a-and-predict ion-t ools/)

Hist one prot ein st ruct ure (ht t ps://www.mun.ca/biology/scarr/Hist one_ Prot ein_ St ruct ure.ht m
l)

Hist oneDB 2.0 - Dat abase of hist ones and variant s (ht t ps://www.ncbi.nlm.nih.gov/project s/Hist
oneDB2.0) at NCBI
Retrieved from
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