LisH domain explained

Symbol:LisH
LisH
Pfam:PF08513
Interpro:IPR013720

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]

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]

Notes and References

  1. Kim MH, Cooper DR, Oleksy A, Devedjiev Y, Derewenda U, Reiner O, Otlewski J, Derewenda ZS . The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications . Structure . 12 . 6 . 987–98 . June 2004 . 15274919 . 10.1016/j.str.2004.03.024 . free .
  2. Mateja A, Cierpicki T, Paduch M, Derewenda ZS, Otlewski J . The dimerization mechanism of LIS1 and its implication for proteins containing the LisH motif . J. Mol. Biol. . 357 . 2 . 621–31 . March 2006 . 16445939 . 10.1016/j.jmb.2006.01.002 .
  3. Gerlitz G, Darhin E, Giorgio G, Franco B, Reiner O . Novel functional features of the Lis-H domain: role in protein dimerization, half-life and cellular localization . Cell Cycle . 4 . 11 . 1632–40 . November 2005 . 16258276 . 10.4161/cc.4.11.2151. free .
  4. Cerna D, Wilson DK . The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex. . J Mol Biol . 2005 . 351 . 4 . 923–35 . 16051270 . 10.1016/j.jmb.2005.06.025 .