Bioquímica. Jeremy M. Berg, John L. Tymoczko, Lubert Stryer. 6a. Edición.

W.H. Freeman and Company. 2007.

Bioquímica. Jeremy M. Berg,
John L. Tymoczko, Lubert
Stryer. 6a. Edición. W.H.
Freeman and Company.
2007.
Bioquímica. Jeremy M. Berg, John L. Tymoczko, Lubert Stryer. 6a. Edición.
W.H. Freeman and Company. 2007.
Bioquímica. Jeremy M. Berg, John L. Tymoczko, Lubert Stryer. 6a. Edición.
W.H. Freeman and Company. 2007.
Bioquímica. Jeremy M. Berg, John L.
Tymoczko, Lubert Stryer. 6a. Edición. W.H.
Freeman and Company. 2007.
Bioquímica. Jeremy M. Berg, John L. Tymoczko, Lubert Stryer. 6a. Edición.
W.H. Freeman and Company. 2007.
Bioquímica. Jeremy M. Berg, John L. Tymoczko, Lubert Stryer. 6a. Edición.
W.H. Freeman and Company. 2007.
Bioquímica. Jeremy M. Berg, John L. Tymoczko, Lubert Stryer. 6a. Edición.
W.H. Freeman and Company. 2007.
Bioquímica. Jeremy M. Berg, John L. Tymoczko, Lubert Stryer. 6a. Edición.
W.H. Freeman and Company. 2007.
Bioquímica. Jeremy M. Berg, John L. Tymoczko, Lubert Stryer. 6a. Edición.
W.H. Freeman and Company. 2007.
Bioquímica. Jeremy M. Berg, John L. Tymoczko, Lubert Stryer. 6a. Edición.
W.H. Freeman and Company. 2007.
Control multidimensional de la
expresión de genes

Dinámica y niveles de
empaquetamiento del ADN
Nucleosoma, soleniodes, asas
cromatinicas y cromosomas
Control epigenético de la
transcripción de genes
Bioquímica. Jeremy M. Berg, John L. Tymoczko, Lubert Stryer. 6a. Edición.
W.H. Freeman and Company. 2007.
https://youtu.be/ccfsV9UYaJU
Cellular DNA is packaged within chromosomes
All eukaryotic cells utilize a similar cycle to
regulate their division
 Chromatin exists in extended and condensed forms

Chromatin,
which is
about half
DNA and
half protein
by mass, is
dispersed
throughout
much of the
nucleus in
Histones, the most abundant proteins in
interphase. chromatin, constitute a family of small, basic
proteins. The five major types of histone proteins
termed Hl, H2A, H2B, H3 and H4 are rich in
positively charged basic amino acids, which
interact with the negatively charged phosphate
groups in DNA.
When chromatin is
extracted from
nuclei and
examined
in the electron
microscope, its
appearance
depends on the salt
concentration to
which it is exposed.
At low salt
concentration
in the absence of
divalent cations
such as Mg +l,
isolated
chromatin
resembles "beads
on a string"
 Nucleosome
consists of a protein
Composed with DNA. The core is
of DNA and an octamer
histones, containing two
copies each of
nucleosomes histones H2A, H2B,
are about 10 H3, and H4.
nm in octameric histone
core is a roughly
diameter disk-shaped
and are the structure.
primary Nucleosomes from
all eukaryotes
structural contain =147 base
units of pairs of DNA
chromatin. wrapped one and
two-thirds turns
around the protein
core.
 The length of
the linker DNA
is more
variable
among
species, and
even
between
different cells
of one
organism,
ranging from
about
10 to 90 base
pairs.
 Structure of the 30-nm fiber

If chromatin is isolated at physiological salt

concentration, it assumes a more condensed
fiberlike form that is 30 nm in diameter.
 If chromatin is isolated at physiological salt
concentration, it assumes a more condensed
fiberlike form that is 30 nm in diameter
 The 30-nm
"zig-zag fibers
ribbon" include H1,
structure the fifth
that is major
wound into histone. H1
a "two- is bound to
start" helix the DNA as
made from it enters
two and exits
"strands" of the
nucleosom nucleosom
es stacked e core.
on top of
each other
like coins.
The chromatin in
chromosomal
regions that are not
being
transcribed or
replicated exists
predominantly in
the condensed,
30-nm fiber form
and in higher-order
folded structures.
The general
structure
of chromatin
is similar in
the cells of all
eukaryotes:
fungi, plants,
and animals.
The
structure of
chromatin
was
optimized
early in the
evolution of
eukaryotic
cells.
The amino acid sequences for four histones (H2A,
H2B, H3, and H4) are highly conserved between
distantly related species.
The amino acid sequence of H1, varies more from
organism to organism.

The similarity in sequence among histones from all

eukaryotes suggests that they fold into very similar
three-dimensional conformations, which were
optimized for histone function early in evolution in a
common ancestor of all modern eukaryotes.
 Modifications of histone tails control chromatin
condensation and function

Histones of
nucleosome core
contains a flexible N-
terminus of 19-39
residues extending
from the globular
structure of the
nucleosome; the H2A
and H2B proteins also
contain a flexible C-
terminus extending
from the globular
histone octamer core.
These termini, called
histone
Tails. The histone tails are required for chromatin to
condense from the beads-on-a-string
conformation into the 30 nm fiber.
Histone H4,
(lysine16) are
critical for
forming the 30-
nm fiber. This
positively
charged lysine
interacts with a
negative patch
at the H2A-H2B
interface of the
next
nucleosome in
the stacked
nucleosomes of
the 30-nm fiber.
Histone tails
are suject to
multiple post-
translational
Modifications.

Histones in a
single
nucleosome
usually contain
several of these
modifications
simultaneously.
Each of these post-translational modifications
contributes to the binding of chromatin-
associated proteins that participate in the
control of chromatin folding and the ability of
DNA and RNA polymerases to replicate or
transcribe or repair the DNA.
 Condensed
regions of
chromatin :
heterochromatin.
Less condensed
chromatin known
as euchromatin.

Heterocromatine: compacted state during interphase and

usually associating with the nuclear envelope, nucleoli, and distinct
foci. In centromeres and telomeres of chromosomes, as well as
transcriptionally inactive genes.
 Heterochromatin
contains H3
methylated on
Lys9 or 27.
Euchromatin H3
acetylated on Lys
9 and 14
methylation of
lysine 4, and
phosphorylation of
serine 10.
 Non-histone proteins organize long
chromatin loops

Some sequences on
DNA are separated by
millions of base pairs
in linear
DNA appeared
reproducibly very
close to one another
since chromatin is
arranged in large
loops which are close
to regions of
chromatin called
scaffold-associated
regions (SA Rs) or
matrix-attachment
regions (MARs). Chromatin loops ranging in size from 1
million to 4 million base pairs in
mammalian interphase cells.
SARs/MARs are
found between the bases of
transcription
units, and genes
chromatin loops
are located in interphase
primarily within chromosomes
the chromatin may be held the
loops. Some
SARs/MARs
structural
function as maintenance
insulators, that is, of chromosome
DNA proteins or smc
sequences of
tens to hundreds
proteins.
of base pairs
that separate
transcription
units from each
other.
Metaphase chromosome structure

Condensation of
chromosomes
during prophase
may involve the
formation of many
more loops of
chromatin, so that
the length of each
loop is
greatly reduced
compared to that
in interphase cells.
Chromonema
fiber then folds
into a structure
with a diameter
of 200-250 nm
called a middle
prophase
chromatid,
which then folds
into the
500- to 750-nm-
diameter
chromatids
observed during
metaphase.