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Chromatin compaction in terminally differentiated avian blood cells: the role of linker histone H5 and non-histone protein MENT.

Kowalski A, Pałyga J - Chromosome Res. (2011)

Bottom Line: Chromatin has a tendency to shift from a relatively decondensed (active) to condensed (inactive) state during cell differentiation due to interactions of specific architectural and/or regulatory proteins with DNA.These highly abundant proteins assist in folding of nucleosome arrays and self-association of chromatin fibers into compacted chromatin structures.Here, we briefly review structural aspects and molecular mode of action by which these unrelated proteins can spread condensed chromatin to form inactivated regions in the genome.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry and Genetics, Institute of Biology, Jan Kochanowski University, ul. Świętokrzyska 15, 25-406 Kielce, Poland. a.kowalski@ujk.kielce.pl

ABSTRACT
Chromatin has a tendency to shift from a relatively decondensed (active) to condensed (inactive) state during cell differentiation due to interactions of specific architectural and/or regulatory proteins with DNA. A promotion of chromatin folding in terminally differentiated avian blood cells requires the presence of either histone H5 in erythrocytes or non-histone protein, myeloid and erythroid nuclear termination stage-specific protein (MENT), in white blood cells (lymphocytes and granulocytes). These highly abundant proteins assist in folding of nucleosome arrays and self-association of chromatin fibers into compacted chromatin structures. Here, we briefly review structural aspects and molecular mode of action by which these unrelated proteins can spread condensed chromatin to form inactivated regions in the genome.

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A domain structure for histone H5 and MENT molecules. While the histone H5 is composed of a globular domain (GD, residues 23–101) flanked by an N-terminal domain (NtD, residues 1–22) and C-terminal domain (CtD, residues 102–189), the MENT possesses an M-loop domain (M-loop, residues 61–91), nuclear localization signal domain (NLS, residues 80–84), and reactive center loop domain (RCL, residues 352–379)
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Fig1: A domain structure for histone H5 and MENT molecules. While the histone H5 is composed of a globular domain (GD, residues 23–101) flanked by an N-terminal domain (NtD, residues 1–22) and C-terminal domain (CtD, residues 102–189), the MENT possesses an M-loop domain (M-loop, residues 61–91), nuclear localization signal domain (NLS, residues 80–84), and reactive center loop domain (RCL, residues 352–379)

Mentions: Histone H5, a member of a linker histone family, is a 20.5-kDa protein containing 189 amino acid. This protein is divided into three distinct structural domains (Briand et al. 1980) (Fig. 1). While the N-terminal domain (NtD), residues 1–21, contains most of the hydrophobic residues and all aromatic residues, the strongly basic C-terminal domain (CtD), residues 101–189, possesses on average 50% Lys and Arg residues (Briand et al. 1980). Both H5 terminal tails are separated by a central globular domain (GD), residues 22–100, which has a winged-helix fold consisting of three helix bundles, H1 (residues 29–38), H2 (residues 48–58) and H3 (residues 65–78), and two β-ribbon strands (residues 81–85 and 93–96) (Ramakrishnan et al. 1993).Fig. 1


Chromatin compaction in terminally differentiated avian blood cells: the role of linker histone H5 and non-histone protein MENT.

Kowalski A, Pałyga J - Chromosome Res. (2011)

A domain structure for histone H5 and MENT molecules. While the histone H5 is composed of a globular domain (GD, residues 23–101) flanked by an N-terminal domain (NtD, residues 1–22) and C-terminal domain (CtD, residues 102–189), the MENT possesses an M-loop domain (M-loop, residues 61–91), nuclear localization signal domain (NLS, residues 80–84), and reactive center loop domain (RCL, residues 352–379)
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3139888&req=5

Fig1: A domain structure for histone H5 and MENT molecules. While the histone H5 is composed of a globular domain (GD, residues 23–101) flanked by an N-terminal domain (NtD, residues 1–22) and C-terminal domain (CtD, residues 102–189), the MENT possesses an M-loop domain (M-loop, residues 61–91), nuclear localization signal domain (NLS, residues 80–84), and reactive center loop domain (RCL, residues 352–379)
Mentions: Histone H5, a member of a linker histone family, is a 20.5-kDa protein containing 189 amino acid. This protein is divided into three distinct structural domains (Briand et al. 1980) (Fig. 1). While the N-terminal domain (NtD), residues 1–21, contains most of the hydrophobic residues and all aromatic residues, the strongly basic C-terminal domain (CtD), residues 101–189, possesses on average 50% Lys and Arg residues (Briand et al. 1980). Both H5 terminal tails are separated by a central globular domain (GD), residues 22–100, which has a winged-helix fold consisting of three helix bundles, H1 (residues 29–38), H2 (residues 48–58) and H3 (residues 65–78), and two β-ribbon strands (residues 81–85 and 93–96) (Ramakrishnan et al. 1993).Fig. 1

Bottom Line: Chromatin has a tendency to shift from a relatively decondensed (active) to condensed (inactive) state during cell differentiation due to interactions of specific architectural and/or regulatory proteins with DNA.These highly abundant proteins assist in folding of nucleosome arrays and self-association of chromatin fibers into compacted chromatin structures.Here, we briefly review structural aspects and molecular mode of action by which these unrelated proteins can spread condensed chromatin to form inactivated regions in the genome.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry and Genetics, Institute of Biology, Jan Kochanowski University, ul. Świętokrzyska 15, 25-406 Kielce, Poland. a.kowalski@ujk.kielce.pl

ABSTRACT
Chromatin has a tendency to shift from a relatively decondensed (active) to condensed (inactive) state during cell differentiation due to interactions of specific architectural and/or regulatory proteins with DNA. A promotion of chromatin folding in terminally differentiated avian blood cells requires the presence of either histone H5 in erythrocytes or non-histone protein, myeloid and erythroid nuclear termination stage-specific protein (MENT), in white blood cells (lymphocytes and granulocytes). These highly abundant proteins assist in folding of nucleosome arrays and self-association of chromatin fibers into compacted chromatin structures. Here, we briefly review structural aspects and molecular mode of action by which these unrelated proteins can spread condensed chromatin to form inactivated regions in the genome.

Show MeSH