IGH Home


Lab Home

Research


Publications


Members


Lab Goodies


Teaching


Imaging



   science links
Science links


Cavalli lab
The Polycomb and Trithorax page

other links
Other links

 
In this page you will find basic information on Polycomb and Trithorax proteins in epigenetic regulation; as well as the teaching material of our lab on this and related subjects. This teaching material can be downloaded and used without need of permission, but please cite this web publication address as the source of information in order to allow users to address us enquiries and correspondence.
You will also find some links to relevant papers in the Polycomb and Trithorax field, and to Web sources of information in this subject. Enjoy polycomb!



Index
Part 1
Polycomb history and introduction
Part 2
Polycomb and trithorax group proteins
Part 3
Landmark Polycomb and trithorax discoveries
Part 4
In-house developed Polycomb tutorials
Part 5
External Polycomb Links
Part 6 Other teaching material
Part 7
Montpellier teaching

  See Polycomb in action "on the fly": Link to the Polycomb and Trithorax genome browser

We have mapped the distribution of Polycomb and Trithorax proteins, several of their sequence specific DNA-binding recruiter proteins, and of their associated histone marks. We also compiled related published data from other labs. Click on the link above to access the genome browser containing these data. This browser is the companion website of the paper  Schuettengruber et al. (2009), PloS Biol, 7(1): e1000013. doi:10.1371/journal.pbio.1000013



The Polycomb and Trithorax World


Top PART 1.    History

Polycomb group (PcG) and trithorax group (trxG) proteins regulate expression  patterns of many developmental genes. Their function is best understood in the regulation of homeotic genes, where these proteins are able to maintain, respectively, silenced or active states throughout development. These proteins raised considerable interest in recent years, both because the basic regulatory mechanisms that involve these factors are fascinating, and because they play key roles in a variety of normal cellular processes and in disease.


A brief introduction to Polycomb and Trithorax:

Polycomb group (PcG) proteins are highly conserved regulatory factors that were initially discovered in Drosophila. PcG genes are best known for their role in maintaining silent expression states of Hox genes during development, while trithorax group (trxG) proteins maintain Hox gene expression patterns in the appropriate spatial domains. PcG and trxG proteins are also involved in the regulation of normal cell proliferation, and their mutation has been linked to defects in stem cell fates and to cancer. They act by regulating chromatin structure and chromosome architecture at their target loci.

PcG proteins form multimeric complexes that exert their functions by modifying chromatin structure and by regulating the deposition and recognition of multiple post-translational histone  modifications. Three major PcG protein complexes have been described. The first, named PhoRC, contains the DNA-binding protein Pho (this is the Drosophila name, the homolog in mammals is YY1). The second complex, named the E(Z)/ESC complex or Polycomb Repressive Complex 2 (PRC2), contains four core proteins: the histone methyltransferase Enhancer of Zeste (E(Z)), Extra sex combs (ESC), Suppressor of zeste-12 (SU(Z)12), and nucleosome-remodeling factor 55 (NURF-55). E(Z) trimethylates lysine 27 of histone H3 (H3K27me3), and, to a lesser extent, lysine 9 of histone H3 (H3K9me3). A third complex, named PRC1, recognizes these methylation marks via the chromodomain of the Polycomb (PC) protein. PC is a stoichiometric component of PRC1, together with Polyhomeotic (PH), Posterior Sex Combs (PSC), and dRING. In mammals, the duplication of many PcG genes allows variations in complex composition, which differ with cell type and developmental stage.

TrxG proteins are a somewhat heterogeneous group, but they are characterized by complementary mechanistic properties to the PcG. Within trxG members, some bind specific sequences of DNA. A second class class of trxG members is composed by SET domain factors like Drosophila Trx and Ash1 and vertebrate MLL, as well as their associated proteins. A third class of trxG factors comprises protein components of ATP-dependent chromatin remodeling complexes like the SWI/SNF or the NURF complexes, and includes proteins (such as one component of the NURF complex) specifically capable to "read" the histone methylation marks laid down by the SET domain proteins.

In Drosophila, PcG proteins repress their target genes by binding to specific DNA elements called Polycomb Response Elements (PREs). Analysis of known PREs has revealed the presence of binding sites (usually in multiple copies) for several DNA-binding proteins, such as Pleihomeotic (PHO) and Pleihomeotic-like (PHOL), GAGA factor (GAF)/Pipsqueak (PSQ), Zeste and DSP. Other studies have suggested possible additional roles for other proteins, such as the corepressor CtBP and the DNA binding factors Grainyhead (GRH) as well as members of the Sp1/KLF family. Therefore, a large number of proteins might contribute to PcG recruitment at PREs. Each PRE has a different number and topological organization of binding sites for these factors, possibly providing the basis for the specificity of PRE function.

PREs have only been characterized in Drosophila so far. In general, PREs might be simply defined as DNA elements necessary and sufficient for recruitment of PcG complexes and for PcG-dependent silencing of flanking promoters. Many of the PcG binding sites identified by chromatin immunoprecipitation in vertebrates might correspond to this criterion. Their DNA sequences are likely to be fairly different from fly PREs, since three of the DNA-binding factors involved in PcG recruitment, GAF, Pipsqueak and Zeste, are not conserved in vertebrates.

In addition to modifications at the chromatin level, regulation at the level of nuclear architecture influences the regulation of PcG target genes. In mice, it has been reported that nuclear re-organization is coupled to Hox gene activation in early development. In Drosophila, homologous chromosomes pair in interphase nuclei, and transgenic PREs typically silence more strongly when they are present in two copies on homologous chromosomes. This notion of pairing is reinforced by the finding that PRE-containing sequences can also pair with homologous sequences located on different chromosomes, and that these long distance nuclear interactions reinforce PcG-mediated silencing.

Therefore, multiple mechanisms cooperate to drive regulation of gene expression by PcG and trxG proteins. This is likely very important in light of the fact that these proteins regulate a large number of genes, sometimes maintaining the memory of transcriptional states, while in other cases their regulation is more flexible. These multiple mechanisms may be important to ensure the necessary regulatory plasticity, while providing sufficient robustness to the regulated state.

Recent reviews for further readings

1: Lanzuolo C, Orlando V.

Memories from the polycomb group proteins
Annu Rev Genet. 2012;46:561-89. doi: 10.1146/annurev-genet-110711-155603. Epub 2012 Sep 17.
PMID: 22994356 [PubMed - in process]

2: Pirrotta V, Li HB.

A view of nuclear Polycomb bodies.
Curr Opin Genet Dev. 2012 Apr;22(2):101-9. doi: 10.1016/j.gde.2011.11.004. Epub 2011 Dec 16. Review.
PMID: 22178420 [PubMed - indexed for MEDLINE]

3: Holec S, Berger F

Polycomb group complexes mediate developmental transitions in plants.
Plant Physiol. 2012 Jan;158(1):35-43. doi: 10.1104/pp.111.186445. Epub 2011 Nov 15. Review. No abstract available.
PMID: 22086420 [PubMed - indexed for MEDLINE] 

4: Bantignies F, Cavalli G

Polycomb group proteins: repression in 3D.
Trends Genet. 2011 Nov;27(11):454-64. doi: 10.1016/j.tig.2011.06.008. Epub 2011 Jul 25. Review.
PMID: 21794944 [PubMed - indexed for MEDLINE]

5:
Fisher CL, Fisher AG.

Chromatin states in pluripotent, differentiated, and reprogrammed cells.
Curr Opin Genet Dev. 2011 Apr;21(2):140-6. doi: 10.1016/j.gde.2011.01.015. Review.
PMID: 21316216 [PubMed - indexed for MEDLINE]

6: Schuettengruber B, Martinez AM, Iovino N, Cavalli G.

Trithorax group proteins: switching genes on and keeping them active.
Nat Rev Mol Cell Biol. 2011 Nov 23;12(12):799-814. doi: 10.1038/nrm3230. Review.
PMID: 22108599 [PubMed - indexed for MEDLINE]

7: Margueron R, Reinberg D.

The Polycomb complex PRC2 and its mark in life.
Nature. 2011 Jan 20;469(7330):343-9. doi: 10.1038/nature09784. Review.
PMID: 21248841 [PubMed - indexed for MEDLINE]

8: Beisel C, Paro R.

Silencing chromatin: comparing modes and mechanisms.
Nat Rev Genet. 2011 Feb;12(2):123-35. doi: 10.1038/nrg2932. Epub 2011 Jan 11. Review.
PMID: 21221116 [PubMed - indexed for MEDLINE]

9: Sawarkar R, Paro R.

Interpretation of developmental signaling at chromatin: the Polycomb perspective.
Dev Cell. 2010 Nov 16;19(5):651-61. doi: 10.1016/j.devcel.2010.10.012. Review.
PMID: 21074716 [PubMed - indexed for MEDLINE]

10: Mills AA.

Throwing the cancer switch: reciprocal roles of polycomb and trithorax proteins.
Nat Rev Cancer. 2010 Oct;10(10):669-82. doi: 10.1038/nrc2931. Review.
PMID: 20865010 [PubMed - indexed for MEDLINE]

11: Sauvageau M, Sauvageau G.

Polycomb group proteins: multi-faceted regulators of somatic stem cells and cancer.
Cell Stem Cell. 2010 Sep 3;7(3):299-313. doi: 10.1016/j.stem.2010.08.002. Review.
PMID: 20804967 [PubMed - indexed for MEDLINE]

12: Schuettengruber B, Chourrout D, Vervoort M, Leblanc B, Cavalli G.

Genome regulation by polycomb and trithorax proteins.
Cell. 2007 Feb 23;128(4):735-45.
PMID: 17320510 [PubMed - in process]






Top PART 2.   Polycomb and Trithorax group proteins

This table lists PcG and trxG proteins in humans and flies, as well as proteins that may be involved at recruiting them to their target genes. The left column indicates whether the proteins are found in well-characterized biochemical complexes. A brief note describes the main function of each protein. In the Pubmed links column, main papers describing the proteins are hyperlinked. When too many papers have been published on a given protein, I have put a link to a review discussing it in more detail.

*
indicates that the protein exist but its function in the PcG or trxG pathway is still not clear

Note: This table is constantly under revision. should you see mistakes or have updates, please send me an email

Drosophila melanogaster
Homo sapiens
Notes
PcG/trxG recruiters




Dsp1 HMGB2 Dsp1 is an HMG box protein. It assists Pho in PcG recruitment at Drosophila PREs.
HMGB2 is involved in YY1 in silencing of D4Z4 repeats

Grh
GRHL1
Fly Grh helps PcG recruitment at one PRE

Gaga factor / Trl
?
Fly Trl is involved for PcG recruitment at some PREs although is classified as a trxG protein. It is a Zn-finger sequence specific protein that binds the GAGAG motif. It also contains a BTP/POZ domain that is generally involved in protein-protein interactions

Lolal
?
Lola-like binds Trl and acts as a PcG protein

Psq
?
Psq co-purifies with components of the PRC1 complex and binds the same sequences as Trl

Zeste
?
Zeste found within PRC1 but also linked to trxG-mediated activation


Fly
PhoRC complex


Identified in 2006
Pho
YY1 *
Fly PhoRC binds PREs and is involved in recruitment of PcG proteins to PREs. Pho also forms a second complex named INO80, likely to be involved in chromatin remodelling.
Pho can recruit the histone methyltransferase E(z) to the Ubx PRE. In vitro, it can also recruit PRC1 components to DNA independent on the action of E(z).
Whether PhoRC exist in human cells is unknown, but its homolog YY1 ca, recruit PcG proteins to target genes

Phol
YY2 *
dSfmbt (CG16975)
L3MBTL2 *

?
E2F6
E2F6 forms two different multimeric complexes containing PcG proteins, one with RING1A, RING1B and MBLR, and the other one with EZH2, E(PC) and Sin3A

?
BCL6
BCL6 is a BTB containing protein (similar to Drosophila Krüppel, but it is not known whether it is a true homolog) that was suggested to recruit PcG proteins to its target genes via the corepressor BCOR complex

Rbf

RB1
RBL1
Human Retinoblastoma protein represses genes in a PcG-dependent manner to block cell proliferation. This pathway was not yet identified in other organisms

?
PLZF
PLZF has been shown to bind to the HoxD complex and to bind Polycomb proteins on chromatin. This sequence specific DNA binding protein contains a Zn-Finger domain and a BPB/POZ domain that is generally involved in protein-protein interactions. Plzf mutants strongly derepress the HoxD locus in the embryonic hindlimb bud, PLZF binds to Bmi-1 and recruits it to HoxD
PcG complexes







PRC2 complex


H3K27 trimethylation activity characterized in 2002



E(z)
EZH2

EZH1
SET domain histone methyltransferase, specific for H3K27.


Esc
EED
EED is required for the histone methyltransferase activity of EZH2 within the PRC2 complex
Escl


Su(z)12
SUZ12
Like EED, SUZ12 is a critical minimal component required for enzymatic activity of the PRC2 complexes. In Drosophila, Su(z)12 drives nucleosome binding by PRC2.
Nurf-55 (Caf1)
RBBP4/RbpAp48

RBBP7/RbAp46
Drosophila Nurf55 and Su(z)12 form the minimal nucleosome binding module of PRC2 in vitro





PRC2-associated factors


Pcl
PCL1/PHF1

PCL2/MTF2


PCL3/PHF19/MTF2L1
Pcl was found in a PRC2 complex-subtype in flies, extracted from late developmental stages. This complex has histone deacetylation activity dependent on Rpd3. Pcl is perfectly colocalized with PC in polytene chromosomes, suggesting that it links PRC2 to PRC1.
Rpd3
HDAC2
Sir2
SIRT1
SIRT1 was found in a subtype of PRC2 complex in human and flies, linking polycomb silencing to histone deacetylation and cancer.










PRC1 complex

Identified in 1999.

PC identified as a reader of the H3K27me3 mark in 2002.

H2A ubiquitylation activity found in 2004.












RING1/RING1A/RNF1
RING domain protein that is essential for the H2A ubiquitylation function of RING1B within the hPRC1L complex (see below)
Sce/dRing RNF2/RING1B/RING2
RING1B is the catalytic subunit responsible for the H2A ubiquitylation within the hPRC1L complex. Sce/dRing is the corresponding protein in Drosophila
Pc
CBX2/HPC1/M33

CBX4/HPC2

CBX6

CBX7

CBX8/HPC3/PC3
Chromo domain protein, reader of the H3K27me3 mark. Required for silencing in flies.

In mammals, multiple homologs exert different functions by forming alternate PRC1 complexes (Refs a   b   c)
Ph-p PHC1/EDR1/HPH1

PHC2/EDR2/HPH2

PHC3/EDR3/HPH3
Polyhomeotic proteins are SAM and Zn-finger proteins that are stoichiometric components of PRC1 and required for silencing. In flies, Polyhomeotic has additional phenotypes when compared to Polycomb, suggesting that it may have additional functions.
Flag-tagged Ph and Psc were the starting components leading to the identification of the PRC1 complex in 1999.
Ph-d


Psc
PCGF1 (NSPc1)

PCGF2/RNF110/ZFP144 (MEL18)

PCGF3

PCGF4 (BMI1)

PCGF5

PCGF6 (MBLR)

RING domain protein that is essential for the H2A ubiquitylation function of RING1B. BMI1 is a central component of the hPRC1L complex that contains RING1A, RING1B, HPH2 and PC3. In Drosophila, there is a second gene highly similar to Psc, named Su(z)2, which binds to similar sites in polytene chromosomes (Ref)

In mammals, multiple homologs exert different functions by forming alternate PRC1 complexes (Refs a   b   c)




ZNF134

Scm
SCMH1

TAFs


trxG complexes






SWI/SNF complex

Characterized in 1994

trxG function for Brm discovered in 1992

Brm
SMARCA2/BRM

The Brm complex is a chromatin remodelling complex that uses the energy of ATP to remodel nucleosome structure and/or position, opening up chromatin structure. The Brm protein is the ATP-dependent engine of the complex. Moreover, this protein has a Bromodomain which drives binding to acetylated histones. In human, there are two subcomplexes, containing either BRM or BRG1.  Brm complexes are involved in a large number of gene activation processes, probably beyond their function as  antagonists of PcG-mediated silencing.



SMARCA4/BRG1
Osa
ARID1A/BAF250
mor
SMARCC2/BAF170
Snr1
SMARCB1/hSNF5/BAF47


NURF complex

Identified in 1995
Reader of the H3K4me3 mark identified in 2006
Iswi
SMARCA1/SNF2L/ISWI


The NURF complex, like the Brm complex, is a chromatin remodelling complex that uses the energy of ATP to remodel nucleosome structure and/or position, opening up chromatin structure. The ATP-dependent engine is Iswi/SNF2L in this case. In addition, this complex "reads" the histone H3K4me3 mark via the PHD finger of its largest subunit: Nurf-301/BPTF.

Nurf-38

Nurf-55 (Caf1) RBBP4/RbpAp48

RBBP7/RbAp46
E(bx)/Nurf-301
BPTF

TAC1 complex

Identified in 2001

Trx function in H3K4 methylation found in 2004.
Trx

??? Human homologs exist (see below for Trx homologs MLL1-3), but the homolog complex has not been found. Instead, MLL complexes have been isolated, which are not known in flies.



The TAC1 complex seems to activate transcription of its target genes by stimulating transcription initiation as well as elongation. This occurs at Hox genes, but also at genes that were previously unknown to be regulated by trxG proteins like heat-shock genes. No TAC1-homologous complex has been isolated in human.

nej/dCBP
Sbf1

Ash1 complex
Ash1
??? Homologs exist in human, but it is unknown whether they form a complex

In Drosophila, Ash1 was shown to directly interact with dCBP and activate gene expression.

nej/dCBP



MLL complexes

Identified in 2002


??? Again, fly homologs of the MLL subunits exist, but no MLL complexes have been isolated in flies




MLL/ALL-1/HRX/TRX1
MLL2
MLL3


These are the human Trx complexes. There are most likely multiple MLL complexes, each containing a different MLL subunit, which can function as a H3K4 methyltransferase. It is unclear whether the different MLLs have different functions. The WDR5 subunit binds to methyl H3K4 and stimulates further methylation by the SET domain of MLL. The ASH2L also regulates catalysis of trimethylation by MLL. In yeast, a similar complex exist, called COMPASS.


WDR5
ASH2L
RBBP5/SWD1
C10orf9/CFP1
PcG/trxG related proteins




H3K4 demethylase
Lid
JARID1C/XLMR/SMCX

JARID1B/PLU-1
Lid was classified as a trxG protein, but it has been later shown to possess H3K4 demethylase activity, which would fit better with a PcG activity. This same enzymatic activity is also found in the human proteins RBP2 (Refs a, b), and PCGF6/MBLR/RING6A (Ref).
H3K27 demethylases dUTX
UTX

JMJD3
These proteins were found to be able to demethylated tri- and dimethylated histone H3 K27. Biochemically, the mammalian components associate with MLL (TrxG) complexes. In flies, dUTX colocalizes with the elongating form of RNA pol II. Whether their genetic function is to be classified in the trxG remains to be determined.

Asx
ASXL1
ASXL2
Drosophila Asx gene mutations have both PcG and trxG phenotypes.

TIP60 complex
dom
EP400/P400
The Domino protein has a DNA-dependent ATPase domain and belongs to the SWI/SNF family. It is a member of the Tip60 complex, and is involved in repression of Hox genes in flies. More recently, it has also been involved in histone replacement following DNA-damage.

E(Pc)
EPC1
Chromosomal protein sharing some sites with PC in polytene chromosomes in flies. Like E(z), it behaves as a suppressor of heterochromatin position effect variegation, suggesting that both proteins play a role in heterochromatin in addition to PcG-mediated silencing.

NURD complex
Mi-2
CHD4/Mi-2
Mi-2 is the ATP-dependent engine of the NURD chromatin remodelling complex, which couples nucleosome remodelling to histone deacetylation. Drosophila Mi-2 was  proposed to make a link between transcriptional repression in early embryogenesis and PcG-mediated silencing in late embryogenesis

kis
CHD7
Kismet is a chromodomain containing ATP-dependent helicase. Originally identified in flies as a suppressor of mutant Polycomb phenotypes, it was later shown to be involved in RNA pol II transcriptional elongation. Little is known about the function of the human counterpart CHD7.

tna
ZMIZ1 Tonally is a fly Zn-finger protein that, like kis, suppresses Pc mutant phenotypes and is required for expression of Hox genes. Not much is known about its putative human homologue ZMIZ1.

kto
MED12L/TRAP230/TRALP Drosophila Kohtalo and Skuld encode the homologs of the two largest subunits of "Mediator", a transcriptional coactivator complex. They interact directly and their mutants have the same phenotypes. Their trxG function has not been further characterized sofar.

skd
THRAP2/TRAP240
Skuld/TRAP240. See comment to Kohtalo








Top PART 3.   List of landmark discoveries in the Polycomb and Trithorax field:

Year
Brief description of the main findings
Pubmed link
1978
Ed Lewis's founding  Polycomb paper identifying a role for the Pc gene in the regulation of homeotic genes
go!
1985
Characterization of the trithorax gene as a regulator of homeotic gene expression
Role of PcG proteins in the maintenance of homeotic gene expression, i.e. in the process of "cellular memory"
go!
go!
1988
Antagonism between Polycomb and trithorax genes
go!
1989
Polytene chromosome binding pattern of Pc
go!
1991
Identification of Bmi-1, the first mammalian PcG gene
Role of Bmi-1 in Cancer
go!
go:   a!     b!
1992
Involvement of Trithorax in leukemia
go!
1993
Characterization of PREs in Drosophila
Chromatin IP of Polycomb
go:   a!   b!   c!
go!
1994
Bmi-1 action as a bona fide mammalian PcG protein
go!
1997
Analysis of PcG proteins in plants
PcG proteins and epigenetic regulation of gene expression by "cosuppression"
go!
go!
1999
Purification of the PRC1 complex
Role of PcG in cell proliferation
go!
go!
2000
trxG proteins and histone acetylation
go: a!     b!
2001
Link between PcG proteins and the basal transcriptional machinery
PcG proteins and genomic imprinting in mammals
go: a!     b!
go!
2002
Characterization of the E(z)-Esc / PRC2 complex - Histone methyltransferase activity
trxG proteins and histone methylation
go:   a!   b!   c!   d!
go:   a!     b!
2003
Binding of the PC chromo domain to histone H3 methylated at Lysine 27
PcG proteins and X-inactivation
Polycomb as a Sumo E3 protein
go:   a!     b!
go:   a!     b!
go!
2004
PRC1 proteins mediate histone ubiquitination
Identification of a PRC3 complex related to PRC2 and identification of histone H1 methylation activity
go!
go!
2005
Identification of a link between PcG proteins and DNA methylation
Role for PcG proteins in the phenomenon of transdetermination in Drosophila
go: a!     b!
go: a!     b!
2006
Genome-wide mapping of the downstream target sites for PcG proteins
Drosophila: a!  b!  c!
Human
Mouse
2007
Discovery of H3K27me3 demethylases
a!  b!  c!  d!
2009
1- Crystal structure of EED reveals a mechamism for maintenance of H3K27me3 through the cell cycle (partially supports an earlier work by the Helin lab)
2- Identification and initial characterization of the first mammalian PREs
1a! 1b!

2a! 2b!
2010
Various links between PcG proteins and noncoding RNAs (earlier work had pointed to a link between PcG proteins and a ncRNA in X inactivation, but in 2010 the data were broadly generalized and, in particular, SUZ12 was shown to be an RNA-binding protein.
a!  b!  c!  d!
2012
Identification of alternate mammalian PRC1 complexes, suggesting that each of them may have specific functions
    a!   b!   c!
2014
...will it be it your turn ?

For obvious reasons, this list does not include the work in our lab. For this, please go to the lab publications page. Moreover, this list is certainly not perfect. If you have important additions or updates that you wish to be included, please write me an email.




Top PART 4.    In-house developed Polycomb / Trithorax tutorial material

last update: December 2006

1) An introduction to Polycomb and trithorax

You will find here basic material on the subject, with particular attention to the Drosophila field. Some main protein components of the PcG and the trxG are presented, and their target DNA elements, the Polycomb and trithorax response elements (PREs and TREs), are presented and discussed. Examples  of approaches to study PREs and TREs are given. Please note, this is not intended to present a balanced overview of the field and thus most of the work done by our colleaugues is not directly shown or referred to. I strongly recommend to read one the recent excellent reviews published on the subject in order to deepen the understanding of the issues raised in this introductory slide show.

View the powerpoint presentation

Download the original power point file (5.8 Mb)


2) An example of analysis of a Drosophila PRE/TRE in vivo

This example shows a typical approach that can be used to study molecular requirements for the action of PRE and TRE elements in Drosophila. This approach consists in analyzing specific sequences of PRE/TRE and/or the role of specific PcG or trxG components in transgenic constructs. These particular examples are taken from research done in our lab.

View the powerpoint presentation

Download the original powerpoint file (12.1 Mb)


3) An example of the study of nuclear compartmentalization and Polycomb proteins

This example illustrates that PcG proteins form nuclear compartments, and that a Drosophila PRE/TRE is able to induce long-distance interactions in the three dimensional space of the cell nucleus. These interactions can have functional consequences such as increased, PcG dependent, gene silencing and can be heritable through cell division and meiosis. Moreover, the RNAi machinery affects them, suggesting that other cellular components besides PcG proteins are important for the regulation of the nuclear organization of PcG target genes.

View the powerpoint presentation

Download the original powerpoint file (7.1 Mb)




 
Top PART 5.    External Polycomb / Trithorax Links

There are many! Here I list the most frequently visited by us (and in general by the community). They are public resources links rather than lab links, since the purpose here is not to list researchers in the field. If you feel that your favorite link is missing, just submit it by email.

FLY STUFF
OTHER SPECIES STUFF
  • Human protein database - Polycomb group proteins. Searchable database. Basic information on different PcG proteins available.
  • BioGRID BMI1. Database containing links between Bmi1 and other PcG proteins and "anythingelse". You got one page pre-computed from this link, but then you may navigate your way around...



 
Top PART 6.    Other teaching material


A basic course on chromatin structure and function

The structure of nucleosome and the chromatin fiber as well as the role of post-translational histone modifications are discussed.

Chromatin structure and function basics. View the powerpoint

Chromatin structure and function basics. Download the file (pdf, 19,6 Mb)


A course on the role of the Hsp90 chaperone and of trxG members as capacitors of morphological evolution

This set of slides explores the role of protein chaperons and of chromatin components in buffering environmental and genetic variation and, at the same time, as evolutionary motors that may lead to rapid morphological evolution, and perhaps ultimately to speciation.


Hsp90, epigenetics, and evolution. View the powerpoint

Hsp90, epigenetics, and evolution. Download the file (2.7 Mb)





Top PART 7.    Montpellier teaching

Below, you find teaching courses specifically given to Montpellier students

1) UE Méthodologie, a course for Montpellier students on
: in vivo protein-DNA interactions (ChIP, DamID, 3C, 4C, HiC...)

course held in Spring 2013. Download

2) UE Génomique fonctionnelle.

course held in Autumn 2013. Download


3) TC1 : Information génétique – Epigénétique – Bases mécanistiques.

course held in Autumn 2012. Download


3) Master 2 - P2.2-Module Biologie développement

course held in December 2013. Download




Last update: 18 / 01 / 2014