This domain was first identified in drosophila MSL1 (male-specific lethal 1) PMID:12698291. In drosophila it binds to the histone acetyltransferase males-absent on the first protein (MOF) and to protein male-specific lethal-3 (MSL3) PMID:15141166;PMID:21217699.
This domain was first identified in drosophila MSL1 (male-specific lethal 1) [ (PUBMED:12698291) ]. In drosophila it binds to the histone acetyltransferase males-absent on the first protein (MOF) and to protein male-specific lethal-3 (MSL3) [ (PUBMED:15141166) (PUBMED:21217699) ]. This domain can also be found in KAT8 regulatory NSL complex subunit 1 (KANSL1 or NSL1), which is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription [ (PUBMED:20018852) ].
Family alignment:
There are 1820 PEHE domains in 1820 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing PEHE domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with PEHE domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing PEHE domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Structural basis for MOF and MSL3 recruitment into the dosage compensationcomplex by MSL1.
Nat Struct Mol Biol. 2011; 18: 142-9
Display abstract
The male-specific lethal (MSL) complex is required for dosage compensation inDrosophila melanogaster, and analogous complexes exist in mammals. We reportstructures of binary complexes of mammalian MSL3 and the histoneacetyltransferase (HAT) MOF with consecutive segments of MSL1. MSL1 interactswith MSL3 as an extended chain forming an extensive hydrophobic interface,whereas the MSL1-MOF interface involves electrostatic interactions between theHAT domain and a long helix of MSL1. This structure provides insights into thecatalytic mechanism of MOF and enables us to show analogous interactions of MOFwith NSL1. In Drosophila, selective disruption of Msl1 interactions with Msl3 or Mof severely affects Msl1 targeting to the body of dosage-compensated genes andseveral high-affinity sites, without affecting promoter binding. We propose that Msl1 acts as a scaffold for MSL complex assembly to achieve specific targeting tothe X chromosome.
Evolution of chromatin-remodeling complexes: comparative genomics reveals theancient origin of "novel" compensasome genes.
J Mol Evol. 2003; 56: 527-39
Display abstract
Dosage compensation in Drosophila is mediated by a complex, called compensasome, composed of at least five proteins and two noncoding RNAs. Genes encodingcompensasome proteins have been collectively named male-specific lethals or msls.Recent work showed that three of the Drosophila msls (msl-3, mof, and mle) havean ancient origin. In this study, I describe likely orthologues of the tworemaining msls, msl-1 and msl-2, in several invertebrates and vertebrates. TheMSL-2 protein is the only one found in Drosophila and vertebrate genomes thatcontains both a RING finger and a peculiar type of CXC domain, related to the onepresent in Enhancer of Zeste proteins. MSL-1 also contains two evolutionarilyconserved domains: a leucine zipper and a second characteristic region, describedhere for the first time, which I have called the PEHE domain. These two domainsare present in the likely orthologues of MSL-1 as well as in other genes inseveral invertebrate and vertebrate species. Although it cannot be excluded that the compensasome complex is a recent evolutionary novelty, these results showsthat all msls are found in mammals, suggesting that protein complexes related to the compensasome may be present in mammalian species. Metazoans that lack severalof the msls, such as Caenorhabditis elegans, cannot contain compensasomes. Theevolutionary relationships of the compensasome and the NuA4 complex, anotherchromatin-remodeling complex that contains related subunits, are discussed.
