In molecular biology, the LisH domain (lis homology domain) is a protein domain found in a large number of eukaryotic proteins, from metazoa, fungi and plants that have a wide range of functions. The recently solved structure of the LisH domain in the N-terminal region of LIS1 depicted it as a novel dimerisation motif, and that other structural elements are likely to play an important role in dimerisation.[1][2][3]
| LisH | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 n-terminal domain of lissencephaly-1 protein (lis-1) | |||||||||
| Identifiers | |||||||||
| Symbol | LisH | ||||||||
| Pfam | PF08513 | ||||||||
| InterPro | IPR013720 | ||||||||
| |||||||||
The LisH domain is found in the Saccharomyces cerevisiae SIF2 protein, a component of the SET3 complex which is responsible for repressing meiotic genes In SIF2 the LisH domain has been shown to mediate dimer and tetramer formation.[4] It has been shown that the LisH domain helps mediate interaction with components of the SET3 complex.[4]
References
edit- ^ Kim MH, Cooper DR, Oleksy A, Devedjiev Y, Derewenda U, Reiner O, Otlewski J, Derewenda ZS (June 2004). "The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications". Structure. 12 (6): 987–98. doi:10.1016/j.str.2004.03.024. PMID 15274919.
- ^ Mateja A, Cierpicki T, Paduch M, Derewenda ZS, Otlewski J (March 2006). "The dimerization mechanism of LIS1 and its implication for proteins containing the LisH motif". J. Mol. Biol. 357 (2): 621–31. doi:10.1016/j.jmb.2006.01.002. PMID 16445939.
- ^ Gerlitz G, Darhin E, Giorgio G, Franco B, Reiner O (November 2005). "Novel functional features of the Lis-H domain: role in protein dimerization, half-life and cellular localization". Cell Cycle. 4 (11): 1632–40. doi:10.4161/cc.4.11.2151. PMID 16258276.
- ^ a b Cerna D, Wilson DK (2005). "The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex". J Mol Biol. 351 (4): 923–35. doi:10.1016/j.jmb.2005.06.025. PMID 16051270.