RESUMO
We have identified a novel Drosophila protein, DBP80, that exhibits significant similarity to mouse mDEAD5, yeast TIF1/2, and mammalian eIF-4A. DBP80 is a member of a subclass of DEAD-box proteins that contains a distinct domain, PX(I/R)ILLKR(E/D)EETLEGIKQ(F/Y)(F/Y), in addition to the seven canonical helicase domains.
Assuntos
Proteínas de Drosophila , Drosophila melanogaster/genética , RNA Nucleotidiltransferases/química , Proteínas de Ligação a RNA , Sequência de Aminoácidos , Animais , Sequência Conservada , Evolução Molecular , Feminino , Humanos , Proteínas de Insetos/química , Masculino , Camundongos , Dados de Sequência Molecular , RNA HelicasesRESUMO
Posttranslational acetylation of core histone amino termini has long been associated with transcriptionally active chromatin. Recent reports have demonstrated histone acetyltransferase activity in a small group of conserved transcriptional regulators directly linked to gene activation. In addition, the presence of a putative acetyltransferase domain has been discovered in a group of proteins known as the MYST family (for its founding members MOZ, YBF2/SAS3, SAS2, and Tip60). Members of this family are implicated in acute myeloid leukemia (MOZ), transcriptional silencing in yeast (SAS2 and YBF2/SAS3), HIV Tat interaction in humans (Tip60), and dosage compensation in Drosophila (MOF). In this report, we express a yeast ORF with homology to MYST family members and show it possesses histone acetyltransferase activity. Unlike the other MYST family members in Saccharomyces cerevisiae this gene is essential for growth.