2007
DOI: 10.1038/sj.embor.7401085
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Structural and functional analyses of methyl‐lysine binding by the malignant brain tumour repeat protein Sex comb on midleg

Abstract: Sex comb on midleg (Scm) is a member of the Polycomb group of proteins involved in the maintenance of repression of Hox and other developmental control genes in Drosophila. The two malignant brain tumour (MBT) repeats of Scm form a domain that preferentially binds to monomethylated lysine residues either as a free amino acid or in the context of peptides, while unmodified or di-or trimethylated lysine residues are bound with significantly lower affinity. The crystal structure of a monomethyl-lysinecontaining h… Show more

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Cited by 61 publications
(111 citation statements)
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“…Moreover, most of the recovered lethal L(3)mbt mutations delete or modify the MBT repeats (32), underscoring the relevance of these structures. It is through its MBT repeats that L(3)mbt preferentially binds mono-and dimethylated lysine residues in histones (20,21). The data analyzed here show very little overlap with any particular type of the mono-and dimethylated lysines found in various histones ( Fig.…”
Section: What Are the Necessary And Sufficient Components For L(3)mbtmentioning
confidence: 73%
See 1 more Smart Citation
“…Moreover, most of the recovered lethal L(3)mbt mutations delete or modify the MBT repeats (32), underscoring the relevance of these structures. It is through its MBT repeats that L(3)mbt preferentially binds mono-and dimethylated lysine residues in histones (20,21). The data analyzed here show very little overlap with any particular type of the mono-and dimethylated lysines found in various histones ( Fig.…”
Section: What Are the Necessary And Sufficient Components For L(3)mbtmentioning
confidence: 73%
“…L(3)mbt has intrinsic chromatin binding capabilities, which require the integrity of its second MBT repeat (14)(15)(16). To establish a contributing mode for vertebrate L(3)mbt recruitment, several studies have provided evidence consistent with L(3)mbt preferentially, albeit promiscuously, interacting with most mono-and dimethylated lysine residues of histones, with very low affinity for the non-or trimethylated forms (15,20,21). The available crystal structures provide evidence of how this methylated-lysine histone binding may be mediated and suggest that the arrangement of MBT repeats is required for protein stability, even if only one repeat performs the actual binding (15,16,22).…”
mentioning
confidence: 99%
“…41 In vitro studies using isolated MBT domains and histone peptides have demonstrated a general preference for binding to mono-or di-methylated, over un-or tri-methylated peptides. 27,[42][43][44][45][46][47][48][49] An exception to this general rule is provided by the Caenorhabditis elegans protein LIN-61, which displays specificity toward di-and tri-methylated H3K9 histone peptides. 50 A recent study investigating the MBT domains of all 9 human family members has found that some MBT domains (L3MBTL1, L3MBTL3) recognize mono-and/or di-methyl-lysine in a promiscuous, non-sequence-specific fashion, whereas others (SCML2, L3MBTL4, MBTD1, L3MBTL2) specifically bind to only a few selected histone sequences.…”
Section: -23mentioning
confidence: 99%
“…In Drosophila, only two further MBT domaincontaining proteins exist, Sex comb on midleg (scm) (6,(22)(23)(24) and Sex comb with four MBT domains (sfmbt) (5,13,14). Both are members of Polycomb group-related complexes (scm: PRC1 (22); sfmbt: PhoRC (14)) and are required for repression of Hox gene expression during development.…”
mentioning
confidence: 99%