Correction to: EMBO Rep (2012) 13, 619–630. doi:10.1038/embor.2012.78
In this article, published in the July issue of EMBO reports, the references in Table 1 were listed incorrectly. The corrected table has been reproduced here with the updated references. References 22 and 85 in the text were also incorrect; the corrected references are as follows: 22. Zofall M, Grewal SIS (2007) HULC, a histone H2B ubiquitinating complex, modulates heterochromatin independent of histone H3 lysine 4 methylation in fission yeast. J Biol Chem 282: 14065–14072; 85. Mamnun YM, Katayama S, Toda T (2006) Fission yeast Mcl1 interacts with SCF(Pof3) and is required for centromere formation. Biochem Biophys Res Commun 350: 125–130. The reference previously numbered as 85, on page 628 column 2 line 23, is now reference 86. We apologize for these errors.
Table 1. Roles of E3 ligases in chromatin.
| E3 | Species | Substrate | Process | Mode | Mechanism | Recruitment | References | |
|---|---|---|---|---|---|---|---|---|
| Bre1 | Sc Sp Dm Hs | H2B-K123 | Txn initiation | E | Mono | Recruitment | HMTase | 28,29 |
| Sc Hs | H2B-K123 | Txn elongation | E | Mono | Decompact | FACT? | 25,26,31 | |
| Hs | H2B-K123 | Txn repression | E | Mono | Competition | TFIIS | 23 | |
| MSL2 | Hs | H2B-134 | Txn initiation | E | Mono | Recruitment? | HMTase? Bre1? | 33 |
| RING1B | Dm, Hs | H2A (H2A.Z) | Txn repression | H | Mono | Masking | HTMase, FACT | 42,43 |
| Hs | H2A | Txn repression | H | Mono | Recruitment | PRC1 | 44 | |
| Hs | H2A | Txn de-repress. | H | Mono | Recruitment | ZRF1 | 44 | |
| Hs | H2A | Txn repression | H | Mono | Recruitment | RYBP? | 46 | |
| 2A-HUB | Hs | H2A | Txn repression | H | Mono | Masking | FACT | 38 |
| UBR2 | Mm | H2A | Meiotic silenc. | H | Poly? | Masking? | FACT? | 39 |
| BRCA1 | Hs | H2A | Txn repression | H | Mono | Masking? | FACT? | 40 |
| SCFPof1 | Sp | Ams2 | Histone levels | S | Poly | Degradation | Proteasome | 49 |
| Tom1 | Sc | histones | Histone levels | S | Poly | Degradation | Proteasome | 50 |
| Psh1 | Sc Sp Dm Hs | Cse4 | Histone incorp. | E | Poly | Degradation | Proteasome | 51, 52 |
| SCFPpa | Ds, Hs | CID | Histone incorp. | E | Poly | Degradation | Proteasome | 53 |
| Cul4–Ddb1Cdt2 | Hs | Set8/PR-Set7 | Condensation | E | Poly | Degradation | Proteasome | 57–61 |
| SCFSkp2 | Hs | MLL | Cell cycle | S | Poly | Degradation | Proteasome | 62 |
| APC/C | Hs | MLL | Cell cycle | S | Poly | Degradation | Proteasome | 62 |
| SCFFbx4 | Hs | JMJD2A | Cell cycle | S | Poly | Degradation | Proteasome | 63 |
| Not4 | Sc (Hs) | Jhd2 (JARID1C) | Txn | S | Poly | Degradation | Proteasome | 64 |
| Cul4–Ddb1Cdt2 | Sp | Epe1 | Boundary | H | ? | ? | ? | 65 |
| Cul4–Rik1Raf1/2 | Sp | ? | H3K9me | H | ? | ? | ? | 66–70 |
| Cul4–Ddb1DCAF26 | Nc | ? | H3K9me | H | ? | ? | ? | 71–74 |
| Cul2/5–ELC | Cr | ? | H3K9me | H | ? | ? | ? | 75 |
| Cul4–Ddb1Msi1 | At | ? | H3K27me | H | ? | ? | ? | 76 |
| Cul4–Ddb1EED | Hs | ? | H3K27me | H | ? | ? | ? | 77 |
| Msc1 | Sp | ? | HP1 dynamics | H | ? | ? | ? | 78–83 |
| Cul8–Mms1Mms22 | Sc | Ctf4? | Silencing | H | ? | ? | ? | 84 |
| SCFPof3 | Sp | Mcl1 (Ctf4)? | Silencing | H | ? | ? | ? | 85 |
| APC/C | Sp | ? | H3K9me | H | ? | ? | ? | 86 |
2A-HUB, 2A-histone ubiquitin ligase; APC/C, anaphase promoting complex/cyclosome; At, Arabidopsis thaliana; BRCA1, breast cancer 1; Bre1, brefeldin A sensitivity; Cr, Chlamydomonas reinhardtii; Ctf4, chromosome transmission fidelity; Cul2/4/5/8, Cullin 2/4/5/8; Ddb1, DNA damage-binding protein 1; de-repress., de-repression; Dm, Drosophila melanogaster; E, euchromatin; ELC, elongin E; Epe1, enhancer of position effect 1; H, heterochromatin; Hs, Homo sapiens; incorp., incorporation; Msc1, multi-copy suppressor of Chk1; MSL2, male-specific lethal; Mm, Mus musculus; Mms1, methyl methane sulfonate sensitivity 1; mono, monoubiquitylation; Nc, Neurospora crassa; Not4, negative on TATA; Psh1, Pob3/Spt16/histone associated protein; poly, polyubiquitylation; RING1B, really interesting new gene 1B; S, soluble; Sc, Saccharomyces cerevisiae; SCF, Skp1-Cullin-F-box; Sp, Schizosaccharomyces pombe; Tom1, temperature-dependent organization in mitotic nucleus 1; txn, transcription; UBR2, ubiquitin protein ligase E3 in component n-recognin 2.
