INGInhibitor of growth proteins N-terminal histone-binding |
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| SMART accession number: | SM01408
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| Description: |
Histones undergo numerous post-translational modifications, including acetylation and methylation, at residues which are then probable docking sites for various chromatin remodelling complexes. Inhibitor of growth proteins (INGs) specifically bind to residues that have been thus modified. INGs carry a well-characterised C-terminal PHD-type zinc-finger domain, binding with lysine 4-tri-methylated histone H3 (H3K4me3), as well as this N-terminal domain that binds unmodified H3 tails. Although these two regions can bind histones independently, together they increase the apparent association of the ING for the H3 tail. |
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| Interpro abstract (IPR024610): |
Histones undergo numerous post-translational modifications, including acetylation and methylation, at residues which are then probable docking sites for various chromatin remodelling complexes. Inhibitor of growth proteins (INGs) specifically bind to residues that have been thus modified. INGs carry a well-characterised C-terminal PHD-type zinc-finger domain, binding with lysine 4-tri-methylated histone H3 (H3K4me3), as well as this N-terminal domain that binds unmodified H3 tails. Although these two regions can bind histones independently, together they increase the apparent association of the ING for the H3 tail. This entry represents the N-terminal histone binding domain found in inhibitor proteins.
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| Family alignment: |
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There are 0 ING domains in 0 proteins in SMART's nrdb database.
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Cellular role (predicted cellular role)
Cellular role: signalling
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Chruscicki A, Macdonald VE, Young BP, Loewen CJ, Howe LJ
- Critical determinants for chromatin binding by Saccharomyces cerevisiae Yng1exist outside of the plant homeodomain finger.
- Genetics. 2010; 185: 469-77
- Display abstract
The temporal and spatial regulation of histone post-translational modificationsis essential for proper chromatin structure and function. The Saccharomycescerevisiae NuA3 histone acetyltransferase complex modifies the amino-terminaltail of histone H3, but how NuA3 is targeted to specific regions of the genome isnot fully understood. Yng1, a subunit of NuA3 and a member of the Inhibitor ofGrowth (ING) protein family, is required for the interaction of NuA3 withchromatin. This protein contains a C-terminal plant homeodomain (PHD) finger thatspecifically interacts with lysine 4-trimethylated histone H3 (H3K4me3) in vitro.This initially suggested that NuA3 is targeted to regions bearing the H3K4me3mark; however, deletion of the Yng1 PHD finger does not disrupt the interactionof NuA3 with chromatin or result in a phenotype consistent with loss of NuA3function in vivo. In this study, we uncovered the molecular basis for thediscrepancies in these data. We present both genetic and biochemical evidencethat full-length Yng1 has two independent histone-binding motifs: anamino-terminal motif that binds unmodified H3 tails and a carboxyl-terminal PHDfinger that specifically recognizes H3K4me3. Although these motifs can bindhistones independently, together they increase the apparent association of Yng1for the H3 tail.
Structure (3D structures containing this domain)3D Structures of ING domains in PDB
| PDB code | Main view | Title | | 4afl |  | The crystal structure of the ING4 dimerization domain reveals the functional organization of the ING family of chromatin binding proteins. |
| 5j9q |  | 5J9Q |
| 5j9t |  | 5J9T |
| 5j9u |  | 5J9U |
| 5j9w |  | 5J9W |
Links (links to other resources describing this domain)
