Supplementary material S2
A-
SLEZ1 1 QQRILLSKSEVAGWGAFLKNPVYKNDYLGEYTGELISHREADKRGKIYDRA---NSSFLF
AtSWN 1 QQRILLGKSDVAGWGAFLKNSVSKNEYLGEYTGELISHHEADKRGKIYDRA---NSSFLF
SlEZ2 1 QQKVLLGRSDVSGWGAFLKNTVGKHEYLGEYTGELISHREADKRGKIYDRE---NSSFLF
AtCLF 1 QQRVLLGISDVSGWGAFLKNSVSKHEYLGEYTGELISHKEADKRGKIYDRE---NCSFLF
AtMEA 1 NKKILIGKSDVHGWGAFTWDSLKKNEYLGEYTGELITHDEANERGRIEDRI---GSSYLF
HsEZH1 1 KKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKY---MSSFLF
HsEZH2 1 KKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKY---MCSFLF
DmEZ 1 HKHLLMAPSDIAGWGIFLKEGAQKNEFISEYCGEIISQDEADRRGKVYDKY---MCSFLF
DmTRX 1 KDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRE--RYYDSRGIGCYMF
AtATX1 1 RKRLAFGKSGIHGFGIFAKLPHRAGDMMIEYTGELVRPSIADKREQLIYNSMVGAGTYMF
AtATX3 1 NFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQ--GKDCYLF
AtASHH1 1 YAKTKLIKCEGRGWGLVALEEIKAGQFIMEYCGEVISWKEAKKRAQTYETHG-VKDAYII
AtASHH2 1 YVKFERFQSGKKGYGLRLLEDVREGQFLIEYVGEVLDMQSYETRQKEYAFKG-QKHFYFM
DmASH1 1 APGVERFMTADKGWGVRTKLPIAKGTYILEYVGEVVTEKEFKQRMASIYLN--DTHHYCL
DmSu_Var_3-9 1 VPLVLFKTANGSGWGVRAATALRKGEFVCEYIGEIITSDEANERGKAYDDN---GRTYLF
HsSUV39H1 1 YDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQ---GATYLF
AtSUVH1 1 KVRLEVFKTANRGWGLRSWDAIRAGSFICIYVGEAKDKSKVQQTMANDDYTFDTTNVYNP
AtSUVH2 1 RNRLEVFRSKETGWGVRTLDLIEAGAFICEYAGVVVTRLQAEILSMNGDVMVYPGRFTDQ
*** °
SLEZ1 58 DLND------QYVLDAYRKGDKLKFANHSSNPNCFAKVMLVAG-
AtSWN 58 DLND------QYVLDAQRKGDKLKFANHSAKPNCYAKVMFVAG-
SlEZ2 58 NLND------QFVLDAHRKGDKLKFANHSPVPNCYAKVMMVAG-
AtCLF 58 NLND------QFVLDAYRKGDKLKFANHSPEPNCYAKVIMVAG-
AtMEA 58 TLND------QLEIDARRKGNEFKFLNHSARPNCYAKLMIVRG-
HsEZH1 58 NLNN------DFVVDATRKGNKIRFANHSVNPNCYAKVVMVNG-
HsEZH2 58 NLNN------DFVVDATRKGNKIRFANHSVNPNCYAKVMMVNG-
DmEZ 58 NLNN------DFVVDATRKGNKIRFANHSINPNCYAKVMMVTG-
DmTRX 59 KIDD------NLVVDATMRGNAARFINHCCEPNCYSKVVDILG-
AtATX1 61 RIDD------ERVIDATRTGSIAHLINHSCVPNCYSRVITVNG-
AtATX3 59 KISE------EIVIDATDSGNIARLINHSCMPNCYARIVSMGDG
AtASHH1 60 SLNA------SEAIDATKKGSLARFINHSCRPNCETRKWNVLG-
AtASHH2 60 TLNG------NEVIDAGAKGNLGRFINHSCEPNCRTEKWMVNG-
DmASH1 59 HLDG------GLVIDGQRMGSDCRFVNHSCEPNCEMQKWSVNG-
DmSu_Var_3-9 58 DLDYNTA------QDSEYTIDAANYGNISHFINHSCDPNLAVFPCWIEHL
HsSUV39H1 58 DLDY------VEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNL
AtSUVH1 61 FKWNYEPGLADEDACEEMSEESEIPLPLIISAKNVGNVARFMNHSCSPNVFWQPVSYENN
AtSUVH2 61 WRNWGDLSQVYPDFVRPN-YPSLPPLDFSMDVSRMRNVACYISHSKEPNVMVQFVLHDHN
------
SLEZ1 95 ---DHRVGIFAKERIEASEELFYDYRYGPD
AtSWN 95 ---DHRVGIFANERIEASEELFYDYRYGPD
SlEZ2 95 ---DHRVGIFANERICAGEELFYDYRYEPD
AtCLF 95 ---DHRVGIFAKERILAGEELFYDYRYEPD
AtMEA 95 ---DQRIGLFAERAIEEGEELFFDYCYGPE
HsEZH1 95 ---DHRIGIFAKRAIQAGEELFFDYRYSQA
HsEZH2 95 ---DHRIGIFAKRAIQTGEELFFDYRYSQA
DmEZ 95 ---DHRIGIFAKRAIQPGEELFFDYRYGPT
DmTRX 96 ---HKHIIIFALRRIVQGEELTYDYKFPFE
AtATX1 98 ---DEHIIIFAKRHIPKWEELTYDYRFFSI
AtATX3 97 --EDNRIVLIAKTNVAAGEELTYDYLFEVD
AtASHH1 97 ---EVRVGIFAKESISPRTELAYDYNFEWY
AtASHH2 97 ---EICVGIFSMQDLKKGQELTFDYNYVRV
DmASH1 96 ---LSRMVLFAKRAIEEGEELTYDYNFSLF
DmSu_Var_3-9 102 NVALPHLVFFTLRPIKAGEELSFDYIRADN
HsSUV39H1 99 DERLPRIAFFATRTIRAGEELTFDYNMQVD
AtSUVH1 121 SQLFVHVAFFAISHIPPMTELTYDYGVSRP
AtSUVH2 120 HLMFPRVMLFALENISPLAELSLDYGLADE
-- ---
B-
SLEZ1 1 QQRILLSKSEVAGWGAFLKNPVYKNDYLGEYTGELISHREADKRGKIYDRANSSFLFDLN
PhCLF3 1 QQRILLAKSHVAGWGAFLKNPVNKNDYLGEYTGELISHREADKRGKIYDRANSSFLFDLN
ZmMEZ2 1 QQRILLGRSDVAGWGAFIKNPVNKNDYLGEYTGELISHKEADKRGKIYDRANSSFLFDLN
ZmMEZ3 1 QQRILLGRSDVAGWGAFIKNPVNKNDYLGEYTGELISHKEADKRGKIYDRANSSFLFDLN
OsiEZ1 1 QQRILLGKSDVAGWGAFIKNPVNRNDYLGEYTGELISHREADKRGKIYDRANSSFLFDLN
AtSWN 1 QQRILLGKSDVAGWGAFLKNSVSKNEYLGEYTGELISHHEADKRGKIYDRANSSFLFDLN
ZmMEZ1 1 QQRVLLGRSDVSGWGAFLKNSVSKHEYLGEYTGELISHKEADKRGKIYDRENSSFLFNLN
OsiEZ2 1 QQRVLLGRSDVSGWGAFLKNSVGKHEYLGEYTGELISHKEADKRGKIYDRENSSFLFNLN
AtCLF 1 QQRVLLGISDVSGWGAFLKNSVSKHEYLGEYTGELISHKEADKRGKIYDRENCSFLFNLN
PhCLF2 1 QQRVLLGRSDVSGWGAFLKNSVGKHEYLGEYTGEIISHHEADKRGKIYDREDSSFLFNLN
SlEZ2 1 QQKVLLGRSDVSGWGAFLKNTVGKHEYLGEYTGELISHREADKRGKIYDRENSSFLFNLN
PhCLF1 1 QQKVLLGRSDVSGWGAFLKNSVGKHEYLGEYTGELISHREADKRGKIYDRENSSFLFNLN
DmEZ 1 HKHLLMAPSDIAGWGIFLKEGAQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLN
AtMEA 1 NKKILIGKSDVHGWGAFTWDSLKKNEYLGEYTGELITHDEANERGRIEDRIGSSYLFTLN
*** °
SLEZ1 61 DQYVLDAYRKGDKLKFANHSSNPNCFAKVMLVAGDHRVGIFAKERIEASEELFYDYRYGP
PhCLF3 61 DQYVLDAYRKGDKLKFANHSSNPNCYAKVMLVAGDHRVGIFAKEHIEASQELFYDYRYGP
ZmMEZ2 61 DQYVLDAYRKGDKLKFANHSSNPNCYAKVMLVAGDHRVGIYAKEHIEASEELFYDYRYGP
ZmMEZ3 61 DQYVLDAYRKGDKLKFANHSSNPNCYAKVMLVAGDHRVGIYAKEHIEASEELFYDYRYGP
OsiEZ1 61 EQYVLDAYRKGDKLKFANHSSNPNCYAKVMLVAGDHRVGIYAKDRIEASEELFYDYRYGP
AtSWN 61 DQYVLDAQRKGDKLKFANHSAKPNCYAKVMFVAGDHRVGIFANERIEASEELFYDYRYGP
ZmMEZ1 61 NEYVLDAYRMGDKLKFANHAPDPNCYAKVIMVTGDHRVGIFAKERILAGEELFYDYRYEP
OsiEZ2 61 NEYVLDAYRMGDKLKFANHSPDPNCYAKVIMVAGDHRVGIFAKERISAGEELFYDYRYEP
AtCLF 61 DQFVLDAYRKGDKLKFANHSPEPNCYAKVIMVAGDHRVGIFAKERILAGEELFYDYRYEP
PhCLF2 61 DQFVLDAYRKGDKLKFANHSPAPNCYAKVIMVAGDHRVGIFAKERICAGEELFYDYRYEA
SlEZ2 61 DQFVLDAHRKGDKLKFANHSPVPNCYAKVMMVAGDHRVGIFANERICAGEELFYDYRYEP
PhCLF1 61 DQFVLDAHRKGDKLKFANHSPVPNCYAKVMMVAGDHRVGIFANERICAGEELFYDYRYEP
DmEZ 61 NDFVVDATRKGNKIRFANHSINPNCYAKVMMVTGDHRIGIFAKRAIQPGEELFFDYRYGP
AtMEA 61 DQLEIDARRKGNEFKFLNHSARPNCYAKLMIVRGDQRIGLFAERAIEEGEELFFDYCYGP
------
Fig. S2
A- SET Domain sequence alignment from SET domain proteins belonging to class I (light grey), class II (grey), class III (Black) and Class V (White) of SET domain proteins. Sequence alignment have been performed using clustalW and colored with boxshade. Accession number of proteins is as indicated in Fig 2. Amino acids in red have been shown to abolish the histone methyl transferase when mutated (Rea at al, 2000, Müller et al, 2002, Joshi et al, 2008). Conserved domains corresponding to the ADO Met site, the catalytic site and the pseudo knot are indicated by *, ° and – respectively. Accession number of class I proteins : AtCLF: CAA71599, AtMEA: AAC39446 AtSWN: AAD09108, DmEZ: AAC46462, HsEZH1: EAW60870, HsEZH2:EAL24423, of class II proteins : AtATX1: AAK01237, AtATX3: CAB71104, DmTRX:AAF55041, of class III proteins : AtASHH:AAF04434, AtASHH2: AAC34358, DmASH1: AAF49140 and of class IV proteins : AtSUVH1: AAK28966, AtSUVH2: AAK28967, DmSU(VAR)3-9 : CAB93768, HsSUV39H1: CAG46546.
B- Sequence alignment of the SET domain of class I SET domain proteins. Note the very high level of conservation. This class of SET domain protein include all E(z) proteins.
References:
Joshi P, Carrington EA, Wang L, Ketel CS, Miller EL, Jones RS, Simon JA (2008) Dominant alleles identify SET domain residues required for histone methyltransferase of Polycomb Repressive Complex 2. J Biol Chem 283:27757–27766
Mu¨ller J, Hart CM, Francis NJ, Vargas ML, Sengupta A, Wild B, Miller EL, O’Connor MB, Kingston RE, Simon JA (2002) Histone methyltransferase activity of a Drosophila Polycomb Group repressor complex. Cell 111:197–208
Rea S, Eisenhaber F, O’Carroll D, Strahl BD, Sun Z-W, Schmid M, Opravil S, Mechtler K, Ponting CP, Allis CD, Jenuwein T (2000) Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406:593–599