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Item No. 14775

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The malignant brain tumor (MBT) domain is structurally related to chromatin binding domains, such as chromodomains, tudor domains, and PWWP-domains.1,2 MBT domain-containing proteins have a variable number of MBT repeats. The MBT domains recognize methylated lysines on histone tails with varying degree of specificity for the various methyl marks.1 L3MBTL1, a human homolog of the Drosophila lethal(3)MBT protein, is a member of the polycomb group (PcG) of proteins that functions as a transcriptional repressor.3 L3MBTL1 contains three MBT repeat domains which collectively bind to either histone H3 or H4.1,4 The second and third MBT domains were found to bind preferentially to mono- and dimethylated lysines of histone H3 at lysine 4 (H3K4me1) and histone H4 at lysine 20 (H4K20me2).4,5 Recognition of methyl-lysine marks by MBT domains leads to chromatin compaction and a repressed transcriptional state.4,6 Further, L3MBTL1 has a tumor suppressor function and is thought to play a role in maintaining genomic stability and DNA replication.7,8 This protein product contains the MBT repeat region of L3MBTL1.
WARNING This product is not for human or veterinary use.
1. Beyond histone methyl-
2. The Tudor domain 'Royal Family': Tudor, plant Agenet, Chromo, PWWP and MBT domains. Trends Biochem. Sci. 28(2), 69-74 (2003).
3. The human L(3)MBT polycomb group protein is a transcriptional repressor and interacts physically and functionally with TEL (ETV6). The Journal of Biological Chemisty 278(17), 15412-15420 (2003).
4. L3MBTL1, a histone-
5. Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep. 7(4), 397-403 (2006).
6. Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1. Oncogene 27(31), 4293-4304 (2008).
7. The AAA-
8. L3MBTL1 polycomb protein, a candidate tumor suppressor in del(20q12) myeloid disorders, is essential for genome stability. Proc. Natl. Acad. Sci. USA 107(52), 22552-22557 (2010).